[{"extern":"1","language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"citation":{"ieee":"D. J. Anderson and M. Hetzer, “Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum,” <i>Nature Cell Biology</i>, vol. 9, no. 10. Springer Nature, pp. 1160–1166, 2007.","chicago":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” <i>Nature Cell Biology</i>. Springer Nature, 2007. <a href=\"https://doi.org/10.1038/ncb1636\">https://doi.org/10.1038/ncb1636</a>.","ista":"Anderson DJ, Hetzer M. 2007. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. 9(10), 1160–1166.","short":"D.J. Anderson, M. Hetzer, Nature Cell Biology 9 (2007) 1160–1166.","ama":"Anderson DJ, Hetzer M. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. <i>Nature Cell Biology</i>. 2007;9(10):1160-1166. doi:<a href=\"https://doi.org/10.1038/ncb1636\">10.1038/ncb1636</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” <i>Nature Cell Biology</i>, vol. 9, no. 10, Springer Nature, 2007, pp. 1160–66, doi:<a href=\"https://doi.org/10.1038/ncb1636\">10.1038/ncb1636</a>.","apa":"Anderson, D. J., &#38; Hetzer, M. (2007). Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb1636\">https://doi.org/10.1038/ncb1636</a>"},"pmid":1,"external_id":{"pmid":["17828249"]},"_id":"11115","date_updated":"2024-10-14T11:30:08Z","article_processing_charge":"No","issue":"10","intvolume":"         9","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Nature Cell Biology","volume":9,"date_published":"2007-09-09T00:00:00Z","oa_version":"None","publication_status":"published","publisher":"Springer Nature","article_type":"original","day":"09","page":"1160-1166","scopus_import":"1","author":[{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER"}],"doi":"10.1038/ncb1636","year":"2007","title":"Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum","month":"09","type":"journal_article","keyword":["Cell Biology"],"date_created":"2022-04-07T07:56:04Z","abstract":[{"text":"The formation of the nuclear envelope (NE) around chromatin is a major membrane-remodelling event that occurs during cell division of metazoa. It is unclear whether the nuclear membrane reforms by the fusion of NE fragments or if it re-emerges from an intact tubular network of the endoplasmic reticulum (ER). Here, we show that NE formation and expansion requires a tubular ER network and occurs efficiently in the presence of the membrane fusion inhibitor GTPγS. Chromatin recruitment of membranes, which is initiated by tubule-end binding, followed by the formation, expansion and sealing of flat membrane sheets, is mediated by DNA-binding proteins residing in the ER. Thus, chromatin plays an active role in reshaping of the ER during NE formation.","lang":"eng"}],"status":"public","quality_controlled":"1"},{"day":"02","scopus_import":"1","page":"316-332","author":[{"first_name":"M. A.","last_name":"D’Angelo","full_name":"D’Angelo, M. A."},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"doi":"10.1007/s00018-005-5361-3","year":"2006","article_type":"review","title":"The role of the nuclear envelope in cellular organization","month":"01","date_created":"2022-04-07T07:56:22Z","abstract":[{"text":"Over the last years it has become evident that the nuclear envelope (NE) is more than a passive membrane barrier that separates the nucleus from the cytoplasm. The NE not only controls the trafficking of macromolecules between the nucleoplasm and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton to the nuclear periphery. Targeting of chromatin to the NE might actually be part of gene expression regulation in eukaryotes. Mutations in certain NE proteins are associated with a diversity of human diseases, including muscular dystrophy, neuropathy, lipodistrophy, torsion dystonia and the premature aging condition progeria. Despite the importance of the NE for cell division and differentiation, relatively little is known about its biogenesis and its role in human diseases. It is our goal to provide a comprehensive view of the NE and to discuss possible implications of NE-associated changes for gene expression, chromatin organization and signal transduction.","lang":"eng"}],"type":"journal_article","keyword":["Cell Biology","Cellular and Molecular Neuroscience","Pharmacology","Molecular Biology","Molecular Medicine"],"status":"public","quality_controlled":"1","publication_identifier":{"eissn":["1420-9071"],"issn":["1420-682X"]},"citation":{"ista":"D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular organization. Cellular and Molecular Life Sciences. 63(3), 316–332.","short":"M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006) 316–332.","ama":"D’Angelo MA, Hetzer M. The role of the nuclear envelope in cellular organization. <i>Cellular and Molecular Life Sciences</i>. 2006;63(3):316-332. doi:<a href=\"https://doi.org/10.1007/s00018-005-5361-3\">10.1007/s00018-005-5361-3</a>","mla":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3, Springer Nature, 2006, pp. 316–32, doi:<a href=\"https://doi.org/10.1007/s00018-005-5361-3\">10.1007/s00018-005-5361-3</a>.","apa":"D’Angelo, M. A., &#38; Hetzer, M. (2006). The role of the nuclear envelope in cellular organization. <i>Cellular and Molecular Life Sciences</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00018-005-5361-3\">https://doi.org/10.1007/s00018-005-5361-3</a>","ieee":"M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular organization,” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3. Springer Nature, pp. 316–332, 2006.","chicago":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” <i>Cellular and Molecular Life Sciences</i>. Springer Nature, 2006. <a href=\"https://doi.org/10.1007/s00018-005-5361-3\">https://doi.org/10.1007/s00018-005-5361-3</a>."},"pmid":1,"external_id":{"pmid":["16389459"]},"extern":"1","language":[{"iso":"eng"}],"issue":"3","_id":"11117","date_updated":"2024-10-14T11:30:38Z","article_processing_charge":"No","intvolume":"        63","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Cellular and Molecular Life Sciences","publication_status":"published","publisher":"Springer Nature","date_published":"2006-01-02T00:00:00Z","volume":63,"oa_version":"None"},{"publication":"Annual Review of Cell and Developmental Biology","intvolume":"        21","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_status":"published","publisher":"Annual Reviews","oa_version":"None","date_published":"2005-11-10T00:00:00Z","volume":21,"external_id":{"pmid":["16212499"]},"publication_identifier":{"eissn":["1530-8995"],"issn":["1081-0706"]},"citation":{"chicago":"Hetzer, Martin, Tobias C. Walther, and Iain W. Mattaj. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews, 2005. <a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">https://doi.org/10.1146/annurev.cellbio.21.090704.151152</a>.","ieee":"M. Hetzer, T. C. Walther, and I. W. Mattaj, “Pushing the envelope: Structure, function, and dynamics of the nuclear periphery,” <i>Annual Review of Cell and Developmental Biology</i>, vol. 21. Annual Reviews, pp. 347–380, 2005.","ama":"Hetzer M, Walther TC, Mattaj IW. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. <i>Annual Review of Cell and Developmental Biology</i>. 2005;21:347-380. doi:<a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">10.1146/annurev.cellbio.21.090704.151152</a>","mla":"Hetzer, Martin, et al. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” <i>Annual Review of Cell and Developmental Biology</i>, vol. 21, Annual Reviews, 2005, pp. 347–80, doi:<a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">10.1146/annurev.cellbio.21.090704.151152</a>.","ista":"Hetzer M, Walther TC, Mattaj IW. 2005. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annual Review of Cell and Developmental Biology. 21, 347–380.","short":"M. Hetzer, T.C. Walther, I.W. Mattaj, Annual Review of Cell and Developmental Biology 21 (2005) 347–380.","apa":"Hetzer, M., Walther, T. C., &#38; Mattaj, I. W. (2005). Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">https://doi.org/10.1146/annurev.cellbio.21.090704.151152</a>"},"pmid":1,"language":[{"iso":"eng"}],"extern":"1","date_updated":"2022-07-18T08:57:34Z","article_processing_charge":"No","_id":"11120","abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly specialized membrane that delineates the eukaryotic cell nucleus. It is composed of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) and, in metazoa, the lamina. The NE not only regulates the trafficking of macromolecules between nucleoplasm and cytosol but also provides anchoring sites for chromatin and the cytoskeleton. Through these interactions, the NE helps position the nucleus within the cell and chromosomes within the nucleus, thereby regulating the expression of certain genes. The NE is not static, rather it is continuously remodeled during cell division. The most dramatic example of NE reorganization occurs during mitosis in metazoa when the NE undergoes a complete cycle of disassembly and reformation. Despite the importance of the NE for eukaryotic cell life, relatively little is known about its biogenesis or many of its functions. We thus are far from understanding the molecular etiology of a diverse group of NE-associated diseases."}],"date_created":"2022-04-07T07:56:52Z","keyword":["Cell Biology","Developmental Biology"],"type":"journal_article","quality_controlled":"1","status":"public","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"},{"last_name":"Walther","first_name":"Tobias C.","full_name":"Walther, Tobias C."},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."}],"doi":"10.1146/annurev.cellbio.21.090704.151152","year":"2005","day":"10","page":"347-380","scopus_import":"1","article_type":"original","month":"11","title":"Pushing the envelope: Structure, function, and dynamics of the nuclear periphery"},{"issue":"6","date_updated":"2023-08-01T12:55:54Z","article_processing_charge":"No","_id":"13438","external_id":{"pmid":["11706026"]},"citation":{"chicago":"Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner, Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis Elegans.” <i>Journal of Biological Chemistry</i>. Elsevier, 2002. <a href=\"https://doi.org/10.1074/jbc.m107372200\">https://doi.org/10.1074/jbc.m107372200</a>.","ieee":"J. Fürst <i>et al.</i>, “ICln Ion channel splice variants in Caenorhabditis elegans,” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6. Elsevier, pp. 4435–4445, 2002.","ama":"Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. 2002;277(6):4435-4445. doi:<a href=\"https://doi.org/10.1074/jbc.m107372200\">10.1074/jbc.m107372200</a>","mla":"Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis Elegans.” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6, Elsevier, 2002, pp. 4435–45, doi:<a href=\"https://doi.org/10.1074/jbc.m107372200\">10.1074/jbc.m107372200</a>.","ista":"Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M, König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.","short":"J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella, M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological Chemistry 277 (2002) 4435–4445.","apa":"Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella, E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. Elsevier. <a href=\"https://doi.org/10.1074/jbc.m107372200\">https://doi.org/10.1074/jbc.m107372200</a>"},"publication_identifier":{"issn":["0021-9258"]},"pmid":1,"language":[{"iso":"eng"}],"has_accepted_license":"1","extern":"1","publication_status":"published","publisher":"Elsevier","oa_version":"Published Version","date_published":"2002-02-08T00:00:00Z","volume":277,"publication":"Journal of Biological Chemistry","license":"https://creativecommons.org/licenses/by/4.0/","file_date_updated":"2023-08-01T12:44:09Z","intvolume":"       277","user_id":"ea97e931-d5af-11eb-85d4-e6957dddbf17","acknowledgement":"We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical assistance","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"ddc":["570"],"month":"02","title":"ICln Ion channel splice variants in Caenorhabditis elegans","author":[{"full_name":"Fürst, Johannes","first_name":"Johannes","last_name":"Fürst"},{"full_name":"Ritter, Markus","last_name":"Ritter","first_name":"Markus"},{"first_name":"Jakob","last_name":"Rudzki","full_name":"Rudzki, Jakob"},{"orcid":"0000-0001-8559-3973","first_name":"Johann G","last_name":"Danzl","full_name":"Danzl, Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Gschwentner, Martin","last_name":"Gschwentner","first_name":"Martin"},{"full_name":"Scandella, Elke","last_name":"Scandella","first_name":"Elke"},{"full_name":"Jakab, Martin","first_name":"Martin","last_name":"Jakab"},{"full_name":"König, Matthias","first_name":"Matthias","last_name":"König"},{"full_name":"Oehl, Bernhard","first_name":"Bernhard","last_name":"Oehl"},{"first_name":"Florian","last_name":"Lang","full_name":"Lang, Florian"},{"first_name":"Peter","last_name":"Deetjen","full_name":"Deetjen, Peter"},{"last_name":"Paulmichl","first_name":"Markus","full_name":"Paulmichl, Markus"}],"year":"2002","doi":"10.1074/jbc.m107372200","day":"08","page":"4435-4445","scopus_import":"1","article_type":"original","quality_controlled":"1","status":"public","abstract":[{"lang":"eng","text":"ICln is an ion channel identified by expression cloning using a cDNA library from Madin-Darby canine kidney cells. In all organisms tested so far, only one transcript for the ICln protein could be identified. Here we show that two splice variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover, we show that these two splice variants of the ICln channel protein, which we termed IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent inactivation, whereas the IClnN2-induced currents fully inactivated at positive potentials. The molecular entity responsible for the voltage-dependent inactivation of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation that is similar to the “ball and chain” model proposed for the Shaker potassium channel,i.e. a cluster of positively charged amino acids hinders ion permeation through the channel by a molecular and voltage-dependent interaction at the inner vestibulum of the pore. This hypothesis is supported by the finding that synthetic peptides with the same amino acid sequence as the positive cluster can transform the IClnN1-induced current to the current observed after reconstitution of IClnN2. Furthermore, we show that the nematode ICln gene is embedded in an operon harboring two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2 and functional analysis of the related currents revealed a functional interaction between the two proteins, as evidenced by the fact that the IClnN2-induced current in the presence of Nx was no longer voltage-sensitive. The experiments described indicate that the genome organization in nematodes allows an effective approach for the identification of functional partner proteins of ion channels."}],"date_created":"2023-08-01T12:37:50Z","keyword":["Cell Biology","Molecular Biology","Biochemistry"],"file":[{"success":1,"content_type":"application/pdf","date_created":"2023-08-01T12:44:09Z","file_name":"2002_JBC_Fuerst.pdf","date_updated":"2023-08-01T12:44:09Z","creator":"alisjak","access_level":"open_access","relation":"main_file","file_id":"13439","file_size":798920,"checksum":"13abe20f78eb37ab62beb006f62c69b7"}],"oa":1,"type":"journal_article"},{"date_created":"2022-04-07T07:57:19Z","abstract":[{"lang":"eng","text":"The small GTPase Ran is a key regulator of nucleocytoplasmic transport during interphase. The asymmetric distribution of the GTP-bound form of Ran across the nuclear envelope — that is, large quantities in the nucleus compared with small quantities in the cytoplasm — determines the directionality of many nuclear transport processes. Recent findings that Ran also functions in spindle formation and nuclear envelope assembly during mitosis suggest that Ran has a general role in chromatin-centred processes. Ran functions in these events as a signal for chromosome position."}],"type":"journal_article","keyword":["Cell Biology"],"status":"public","quality_controlled":"1","day":"01","scopus_import":"1","page":"E177-E184","author":[{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"},{"first_name":"Oliver J.","last_name":"Gruss","full_name":"Gruss, Oliver J."},{"last_name":"Mattaj","first_name":"Iain W.","full_name":"Mattaj, Iain W."}],"year":"2002","doi":"10.1038/ncb0702-e177","article_type":"original","title":"The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly","month":"07","intvolume":"         4","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication":"Nature Cell Biology","publication_status":"published","publisher":"Springer Nature","date_published":"2002-07-01T00:00:00Z","volume":4,"oa_version":"None","citation":{"ieee":"M. Hetzer, O. J. Gruss, and I. W. Mattaj, “The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly,” <i>Nature Cell Biology</i>, vol. 4, no. 7. Springer Nature, pp. E177–E184, 2002.","chicago":"Hetzer, Martin, Oliver J. Gruss, and Iain W. Mattaj. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” <i>Nature Cell Biology</i>. Springer Nature, 2002. <a href=\"https://doi.org/10.1038/ncb0702-e177\">https://doi.org/10.1038/ncb0702-e177</a>.","apa":"Hetzer, M., Gruss, O. J., &#38; Mattaj, I. W. (2002). The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb0702-e177\">https://doi.org/10.1038/ncb0702-e177</a>","short":"M. Hetzer, O.J. Gruss, I.W. Mattaj, Nature Cell Biology 4 (2002) E177–E184.","ista":"Hetzer M, Gruss OJ, Mattaj IW. 2002. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nature Cell Biology. 4(7), E177–E184.","ama":"Hetzer M, Gruss OJ, Mattaj IW. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. <i>Nature Cell Biology</i>. 2002;4(7):E177-E184. doi:<a href=\"https://doi.org/10.1038/ncb0702-e177\">10.1038/ncb0702-e177</a>","mla":"Hetzer, Martin, et al. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” <i>Nature Cell Biology</i>, vol. 4, no. 7, Springer Nature, 2002, pp. E177–84, doi:<a href=\"https://doi.org/10.1038/ncb0702-e177\">10.1038/ncb0702-e177</a>."},"publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"pmid":1,"external_id":{"pmid":["12105431"]},"extern":"1","language":[{"iso":"eng"}],"issue":"7","_id":"11123","date_updated":"2022-07-18T08:58:03Z","article_processing_charge":"No"},{"month":"11","title":"Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly","article_type":"original","doi":"10.1038/ncb1201-1086","year":"2001","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER"},{"first_name":"Hemmo H.","last_name":"Meyer","full_name":"Meyer, Hemmo H."},{"last_name":"Walther","first_name":"Tobias C.","full_name":"Walther, Tobias C."},{"first_name":"Daniel","last_name":"Bilbao-Cortes","full_name":"Bilbao-Cortes, Daniel"},{"last_name":"Warren","first_name":"Graham","full_name":"Warren, Graham"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"scopus_import":"1","page":"1086-1091","day":"02","quality_controlled":"1","status":"public","keyword":["Cell Biology"],"type":"journal_article","abstract":[{"lang":"eng","text":"Although nuclear envelope (NE) assembly is known to require the GTPase Ran, the membrane fusion machinery involved is uncharacterized. NE assembly involves formation of a reticular network on chromatin, fusion of this network into a closed NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together with the adaptor p47, has two discrete functions in NE assembly. Formation of a closed NE requires the p97–Ufd1–Npl4 complex, not previously implicated in membrane fusion. Subsequent NE growth involves a p97–p47 complex. This study provides the first insights into the molecular mechanisms and specificity of fusion events involved in NE formation."}],"date_created":"2022-04-07T07:57:42Z","article_processing_charge":"No","date_updated":"2022-07-18T08:58:07Z","_id":"11125","issue":"12","language":[{"iso":"eng"}],"extern":"1","external_id":{"pmid":["11781570"]},"pmid":1,"citation":{"apa":"Hetzer, M., Meyer, H. H., Walther, T. C., Bilbao-Cortes, D., Warren, G., &#38; Mattaj, I. W. (2001). Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb1201-1086\">https://doi.org/10.1038/ncb1201-1086</a>","ista":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. 2001. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biology. 3(12), 1086–1091.","short":"M. Hetzer, H.H. Meyer, T.C. Walther, D. Bilbao-Cortes, G. Warren, I.W. Mattaj, Nature Cell Biology 3 (2001) 1086–1091.","mla":"Hetzer, Martin, et al. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” <i>Nature Cell Biology</i>, vol. 3, no. 12, Springer Nature, 2001, pp. 1086–91, doi:<a href=\"https://doi.org/10.1038/ncb1201-1086\">10.1038/ncb1201-1086</a>.","ama":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. <i>Nature Cell Biology</i>. 2001;3(12):1086-1091. doi:<a href=\"https://doi.org/10.1038/ncb1201-1086\">10.1038/ncb1201-1086</a>","ieee":"M. Hetzer, H. H. Meyer, T. C. Walther, D. Bilbao-Cortes, G. Warren, and I. W. Mattaj, “Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly,” <i>Nature Cell Biology</i>, vol. 3, no. 12. Springer Nature, pp. 1086–1091, 2001.","chicago":"Hetzer, Martin, Hemmo H. Meyer, Tobias C. Walther, Daniel Bilbao-Cortes, Graham Warren, and Iain W. Mattaj. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” <i>Nature Cell Biology</i>. Springer Nature, 2001. <a href=\"https://doi.org/10.1038/ncb1201-1086\">https://doi.org/10.1038/ncb1201-1086</a>."},"publication_identifier":{"issn":["1465-7392"],"eissn":["1476-4679"]},"oa_version":"None","volume":3,"date_published":"2001-11-02T00:00:00Z","publisher":"Springer Nature","publication_status":"published","publication":"Nature Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","intvolume":"         3"},{"month":"01","title":"An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins","article_type":"original","year":"2000","doi":"10.1083/jcb.148.2.293","author":[{"orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."}],"page":"293-304","scopus_import":"1","day":"24","quality_controlled":"1","status":"public","keyword":["Cell Biology"],"type":"journal_article","abstract":[{"text":"Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP) components U1A and U2B′′ is mediated by unusually long and complex nuclear localization signals (NLSs). Here we investigate nuclear import of U1A and U2B′′ in vitro and demonstrate that it occurs by an active, saturable process. Several lines of evidence suggest that import of the two proteins occurs by an import mechanism different to those characterized previously. No cross competition is seen with a variety of previously studied NLSs. In contrast to import mediated by members of the importin-β family of nucleocytoplasmic transport receptors, U1A/U2B′′ import is not inhibited by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate is capable of supporting U1A and U2B′′ import, whereas neither nonhydrolyzable adenosine triphosphate analogues nor GTP can do so. U1A and U2B′′ import in vitro does not require the addition of soluble cytosolic proteins, but a factor or factors required for U1A and U2B′′ import remains tightly associated with the nuclear fraction of conventionally permeabilized cells. This activity can be solubilized in the presence of elevated MgCl2. These data suggest that U1A and U2B′′ import into the nucleus occurs by a hitherto uncharacterized mechanism.","lang":"eng"}],"date_created":"2022-04-07T07:57:49Z","article_processing_charge":"No","date_updated":"2022-07-18T08:58:29Z","_id":"11126","issue":"2","language":[{"iso":"eng"}],"extern":"1","external_id":{"pmid":["10648562"]},"pmid":1,"publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"citation":{"ieee":"M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins,” <i>Journal of Cell Biology</i>, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000.","chicago":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2000. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>.","short":"M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.","ista":"Hetzer M, Mattaj IW. 2000. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology. 148(2), 293–304.","ama":"Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. 2000;148(2):293-304. doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>","mla":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” <i>Journal of Cell Biology</i>, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304, doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>.","apa":"Hetzer, M., &#38; Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>"},"oa_version":"None","volume":148,"date_published":"2000-01-24T00:00:00Z","publisher":"Rockefeller University Press","publication_status":"published","publication":"Journal of Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","intvolume":"       148"},{"extern":"1","language":[{"iso":"eng"}],"pmid":1,"publication_identifier":{"issn":["1097-2765"]},"citation":{"short":"M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular Cell 5 (2000) 1013–1024.","ista":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.","mla":"Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24, doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>.","ama":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. 2000;5(6):1013-1024. doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>","apa":"Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., &#38; Mattaj, I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>","ieee":"M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj, “GTP hydrolysis by Ran is required for nuclear envelope assembly,” <i>Molecular Cell</i>, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.","chicago":"Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss, and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>. Elsevier, 2000. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>."},"external_id":{"pmid":["10911995"]},"_id":"11127","article_processing_charge":"No","date_updated":"2022-07-18T08:58:31Z","issue":"6","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","intvolume":"         5","publication":"Molecular Cell","volume":5,"date_published":"2000-06-01T00:00:00Z","oa_version":"Published Version","publisher":"Elsevier","publication_status":"published","article_type":"original","scopus_import":"1","page":"1013-1024","day":"01","year":"2000","doi":"10.1016/s1097-2765(00)80266-x","author":[{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Daniel","last_name":"Bilbao-Cortés","full_name":"Bilbao-Cortés, Daniel"},{"first_name":"Tobias C","last_name":"Walther","full_name":"Walther, Tobias C"},{"full_name":"Gruss, Oliver J","last_name":"Gruss","first_name":"Oliver J"},{"full_name":"Mattaj, Iain W","last_name":"Mattaj","first_name":"Iain W"}],"title":"GTP hydrolysis by Ran is required for nuclear envelope assembly","month":"06","type":"journal_article","oa":1,"keyword":["Cell Biology","Molecular Biology"],"date_created":"2022-04-07T07:57:59Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/S1097-2765(00)80266-X"}],"abstract":[{"text":"Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE) vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion can be complemented by the addition of Ran loaded with either GTP or GDP but not with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus, generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the extensive membrane fusion events that lead to NE formation.","lang":"eng"}],"status":"public","quality_controlled":"1"}]