---
_id: '14844'
abstract:
- lang: eng
text: 'Many cell functions require a concerted effort from multiple membrane proteins,
for example, for signaling, cell division, and endocytosis. One contribution to
their successful self-organization stems from the membrane deformations that these
proteins induce. While the pairwise interaction potential of two membrane-deforming
spheres has recently been measured, membrane-deformation-induced interactions
have been predicted to be nonadditive, and hence their collective behavior cannot
be deduced from this measurement. We here employ a colloidal model system consisting
of adhesive spheres and giant unilamellar vesicles to test these predictions by
measuring the interaction potential of the simplest case of three membrane-deforming,
spherical particles. We quantify their interactions and arrangements and, for
the first time, experimentally confirm and quantify the nonadditive nature of
membrane-deformation-induced interactions. We furthermore conclude that there
exist two favorable configurations on the membrane: (1) a linear and (2) a triangular
arrangement of the three spheres. Using Monte Carlo simulations, we corroborate
the experimentally observed energy minima and identify a lowering of the membrane
deformation as the cause for the observed configurations. The high symmetry of
the preferred arrangements for three particles suggests that arrangements of many
membrane-deforming objects might follow simple rules.'
acknowledgement: We gratefully acknowledge useful discussions with Casper van der
Wel, help by Yogesh Shelke with PAA coverslip preparation, and support by Rachel
Doherty with particle functionalization. A.A. and D.J.K. would like to thank Timon
Idema and George Dadunashvili for initial attempts to simulate the experimental
system. D.J.K. would like to thank the physics department at Leiden University for
funding the PhD position of A.A. B.M. and A.Š. acknowledge funding by the European
Union’s Horizon 2020 research and innovation programme (ERC starting grant no. 802960).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Ali
full_name: Azadbakht, Ali
last_name: Azadbakht
- first_name: Billie
full_name: Meadowcroft, Billie
id: a4725fd6-932b-11ed-81e2-c098c7f37ae1
last_name: Meadowcroft
orcid: 0000-0003-3441-1337
- first_name: Juraj
full_name: Majek, Juraj
id: 3e6d9473-f38e-11ec-8ae0-c4e05a8aa9e1
last_name: Majek
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Daniela J.
full_name: Kraft, Daniela J.
last_name: Kraft
citation:
ama: Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. Nonadditivity in interactions
between three membrane-wrapped colloidal spheres. Biophysical Journal.
2024;123(3):307-316. doi:10.1016/j.bpj.2023.12.020
apa: Azadbakht, A., Meadowcroft, B., Majek, J., Šarić, A., & Kraft, D. J. (2024).
Nonadditivity in interactions between three membrane-wrapped colloidal spheres.
Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2023.12.020
chicago: Azadbakht, Ali, Billie Meadowcroft, Juraj Majek, Anđela Šarić, and Daniela
J. Kraft. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal
Spheres.” Biophysical Journal. Elsevier, 2024. https://doi.org/10.1016/j.bpj.2023.12.020.
ieee: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, and D. J. Kraft, “Nonadditivity
in interactions between three membrane-wrapped colloidal spheres,” Biophysical
Journal, vol. 123, no. 3. Elsevier, pp. 307–316, 2024.
ista: Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. 2024. Nonadditivity
in interactions between three membrane-wrapped colloidal spheres. Biophysical
Journal. 123(3), 307–316.
mla: Azadbakht, Ali, et al. “Nonadditivity in Interactions between Three Membrane-Wrapped
Colloidal Spheres.” Biophysical Journal, vol. 123, no. 3, Elsevier, 2024,
pp. 307–16, doi:10.1016/j.bpj.2023.12.020.
short: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, D.J. Kraft, Biophysical
Journal 123 (2024) 307–316.
date_created: 2024-01-21T23:00:56Z
date_published: 2024-02-06T00:00:00Z
date_updated: 2025-09-04T11:46:15Z
day: '06'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1016/j.bpj.2023.12.020
ec_funded: 1
external_id:
isi:
- '001185235900001'
pmid:
- '38158654'
file:
- access_level: open_access
checksum: 1c8fe1cf950394875b65b90da86428ff
content_type: application/pdf
creator: dernst
date_created: 2024-07-16T12:09:55Z
date_updated: 2024-07-16T12:09:55Z
file_id: '17266'
file_name: 2024_BiophysicalJournal_Azadbakht.pdf
file_size: 3189926
relation: main_file
success: 1
file_date_updated: 2024-07-16T12:09:55Z
has_accepted_license: '1'
intvolume: ' 123'
isi: 1
issue: '3'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '02'
oa: 1
oa_version: Published Version
page: 307-316
pmid: 1
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Biophysical Journal
publication_identifier:
eissn:
- 1542-0086
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nonadditivity in interactions between three membrane-wrapped colloidal spheres
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 123
year: '2024'
...
---
_id: '9350'
abstract:
- lang: eng
text: Intercellular adhesion is the key to multicellularity, and its malfunction
plays an important role in various developmental and disease-related processes.
Although it has been intensively studied by both biologists and physicists, a
commonly accepted definition of cell-cell adhesion is still being debated. Cell-cell
adhesion has been described at the molecular scale as a function of adhesion receptors
controlling binding affinity, at the cellular scale as resistance to detachment
forces or modulation of surface tension, and at the tissue scale as a regulator
of cellular rearrangements and morphogenesis. In this review, we aim to summarize
and discuss recent advances in the molecular, cellular, and theoretical description
of cell-cell adhesion, ranging from biomimetic models to the complexity of cells
and tissues in an organismal context. In particular, we will focus on cadherin-mediated
cell-cell adhesion and the role of adhesion signaling and mechanosensation therein,
two processes central for understanding the biological and physical basis of cell-cell
adhesion.
acknowledgement: T.S. acknowledges funding by the research program “The Active Matter
Physics of Collective Metastasis,” which is financed by the Dutch Research Council
(NWO).
article_processing_charge: No
article_type: original
author:
- first_name: Feyza N
full_name: Arslan, Feyza N
id: 49DA7910-F248-11E8-B48F-1D18A9856A87
last_name: Arslan
orcid: 0000-0001-5809-9566
- first_name: Julia
full_name: Eckert, Julia
last_name: Eckert
- first_name: Thomas
full_name: Schmidt, Thomas
last_name: Schmidt
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: 'Arslan FN, Eckert J, Schmidt T, Heisenberg C-PJ. Holding it together: when
cadherin meets cadherin. Biophysical Journal. 2021;120:4182-4192. doi:10.1016/j.bpj.2021.03.025'
apa: 'Arslan, F. N., Eckert, J., Schmidt, T., & Heisenberg, C.-P. J. (2021).
Holding it together: when cadherin meets cadherin. Biophysical Journal.
Biophysical Society. https://doi.org/10.1016/j.bpj.2021.03.025'
chicago: 'Arslan, Feyza N, Julia Eckert, Thomas Schmidt, and Carl-Philipp J Heisenberg.
“Holding It Together: When Cadherin Meets Cadherin.” Biophysical Journal.
Biophysical Society, 2021. https://doi.org/10.1016/j.bpj.2021.03.025.'
ieee: 'F. N. Arslan, J. Eckert, T. Schmidt, and C.-P. J. Heisenberg, “Holding it
together: when cadherin meets cadherin,” Biophysical Journal, vol. 120.
Biophysical Society, pp. 4182–4192, 2021.'
ista: 'Arslan FN, Eckert J, Schmidt T, Heisenberg C-PJ. 2021. Holding it together:
when cadherin meets cadherin. Biophysical Journal. 120, 4182–4192.'
mla: 'Arslan, Feyza N., et al. “Holding It Together: When Cadherin Meets Cadherin.”
Biophysical Journal, vol. 120, Biophysical Society, 2021, pp. 4182–92,
doi:10.1016/j.bpj.2021.03.025.'
short: F.N. Arslan, J. Eckert, T. Schmidt, C.-P.J. Heisenberg, Biophysical Journal
120 (2021) 4182–4192.
corr_author: '1'
date_created: 2021-04-25T22:01:30Z
date_published: 2021-10-05T00:00:00Z
date_updated: 2026-06-18T19:47:51Z
day: '05'
ddc:
- '570'
department:
- _id: CaHe
doi: 10.1016/j.bpj.2021.03.025
external_id:
isi:
- '000704646900006'
pmid:
- '33794149'
intvolume: ' 120'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://scholarlypublications.universiteitleiden.nl/access/item%3A3251048/view
month: '10'
oa: 1
oa_version: Published Version
page: 4182-4192
pmid: 1
publication: Biophysical Journal
publication_identifier:
eissn:
- 1542-0086
issn:
- 0006-3495
publication_status: published
publisher: Biophysical Society
quality_controlled: '1'
related_material:
record:
- id: '12368'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: 'Holding it together: when cadherin meets cadherin'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2021'
...
---
OA_place: publisher
OA_type: hybrid
_id: '453'
abstract:
- lang: eng
text: Most kinesin motors move in only one direction along microtubules. Members
of the kinesin-5 subfamily were initially described as unidirectional plus-end-directed
motors and shown to produce piconewton forces. However, some fungal kinesin-5
motors are bidirectional. The force production of a bidirectional kinesin-5 has
not yet been measured. Therefore, it remains unknown whether the mechanism of
the unconventional minus-end-directed motility differs fundamentally from that
of plus-end-directed stepping. Using force spectroscopy, we have measured here
the forces that ensembles of purified budding yeast kinesin-5 Cin8 produce in
microtubule gliding assays in both plus- and minus-end direction. Correlation
analysis of pause forces demonstrated that individual Cin8 molecules produce additive
forces in both directions of movement. In ensembles, Cin8 motors were able to
produce single-motor forces up to a magnitude of ∼1.5 pN. Hence, these properties
appear to be conserved within the kinesin-5 subfamily. Force production was largely
independent of the directionality of movement, indicating similarities between
the motility mechanisms for both directions. These results provide constraints
for the development of models for the bidirectional motility mechanism of fission
yeast kinesin-5 and provide insight into the function of this mitotic motor.
acknowledgement: 'The plasmid for full-length kinesin-1 was a gift from G. Holzwarth
and J. Macosko with permission from J. Howard. We thank I. Lueke and N. I. Cade
for technical assistance. G.P. thanks the Francis Crick Institute, and in particular
the Surrey and Salbreux groups, for their hospitality during his sabbatical stay,
as well as Imperial College London for making it possible. This work was supported
by the Francis Crick Institute, which receives its core funding from Cancer Research
UK (FC001163), the United Kingdom Medical Research Council (FC001163), and the Wellcome
Trust (FC001163), and by Imperial College London. J.R. was also supported by a Sir
Henry Wellcome Postdoctoral Fellowship (100145/Z/12/Z) and T.S. by the European
Research Council (Advanced Grant, project 323042). '
article_processing_charge: No
article_type: original
author:
- first_name: Todd
full_name: Fallesen, Todd
last_name: Fallesen
- first_name: Johanna
full_name: Roostalu, Johanna
last_name: Roostalu
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Gunnar
full_name: Pruessner, Gunnar
last_name: Pruessner
- first_name: Thomas
full_name: Surrey, Thomas
last_name: Surrey
citation:
ama: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. Ensembles of bidirectional
kinesin Cin8 produce additive forces in both directions of movement. Biophysical
Journal. 2017;113(9):2055-2067. doi:10.1016/j.bpj.2017.09.006
apa: Fallesen, T., Roostalu, J., Düllberg, C. F., Pruessner, G., & Surrey, T.
(2017). Ensembles of bidirectional kinesin Cin8 produce additive forces in both
directions of movement. Biophysical Journal. Biophysical Society. https://doi.org/10.1016/j.bpj.2017.09.006
chicago: Fallesen, Todd, Johanna Roostalu, Christian F Düllberg, Gunnar Pruessner,
and Thomas Surrey. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces
in Both Directions of Movement.” Biophysical Journal. Biophysical Society,
2017. https://doi.org/10.1016/j.bpj.2017.09.006.
ieee: T. Fallesen, J. Roostalu, C. F. Düllberg, G. Pruessner, and T. Surrey, “Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement,”
Biophysical Journal, vol. 113, no. 9. Biophysical Society, pp. 2055–2067,
2017.
ista: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. 2017. Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement.
Biophysical Journal. 113(9), 2055–2067.
mla: Fallesen, Todd, et al. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive
Forces in Both Directions of Movement.” Biophysical Journal, vol. 113,
no. 9, Biophysical Society, 2017, pp. 2055–67, doi:10.1016/j.bpj.2017.09.006.
short: T. Fallesen, J. Roostalu, C.F. Düllberg, G. Pruessner, T. Surrey, Biophysical
Journal 113 (2017) 2055–2067.
date_created: 2018-12-11T11:46:33Z
date_published: 2017-11-07T00:00:00Z
date_updated: 2025-08-05T14:08:52Z
day: '07'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.bpj.2017.09.006
external_id:
pmid:
- '29117528'
file:
- access_level: open_access
checksum: 99a2474088e20ac74b1882c4fbbb45b1
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:14:03Z
date_updated: 2020-07-14T12:46:31Z
file_id: '5052'
file_name: IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf
file_size: 977192
relation: main_file
file_date_updated: 2020-07-14T12:46:31Z
has_accepted_license: '1'
intvolume: ' 113'
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '11'
oa: 1
oa_version: Published Version
page: 2055 - 2067
pmid: 1
publication: Biophysical Journal
publication_identifier:
eissn:
- 1542-0086
issn:
- 0006-3495
publication_status: published
publisher: Biophysical Society
publist_id: '7369'
pubrep_id: '965'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions
of movement
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2017'
...