@article{20082,
  abstract     = {Efficient immune responses rely on the capacity of leukocytes to traverse diverse and complex tissues. To meet such changing environmental conditions, leukocytes usually adopt an ameboid configuration, using their forward-positioned nucleus as a probe to identify and follow the path of least resistance among pre-existing pores. We show that, in dense environments where even the largest pores preclude free passage, leukocytes position their nucleus behind the centrosome and organelles. The local compression imposed on the cell body by its surroundings triggers assembly of a central F-actin pool, located between cell front and nucleus. Central actin pushes outward to transiently dilate a path for organelles and nucleus. Pools of central and front actin are tightly coupled and experimental depletion of the central pool enhances actin accumulation and protrusion formation at the cell front. Although this shifted balance speeds up cells in permissive environments, migration in restrictive environments is impaired, as the unleashed leading edge dissociates from the trapped cell body. Our findings establish an actin regulatory loop that balances path dilation with advancement of the leading edge to maintain cellular coherence.},
  author       = {Dos Reis Rodrigues, Patricia and Avellaneda Sarrió, Mario and Canigova, Nikola and Gärtner, Florian R and Vaahtomeri, Kari and Riedl, Michael and De Vries, Ingrid and Merrin, Jack and Hauschild, Robert and Fukui, Yoshinori and Juanes Garcia, Alba and Sixt, Michael K},
  issn         = {1529-2916},
  journal      = {Nature Immunology},
  pages        = {1258–1266},
  publisher    = {Springer Nature},
  title        = {{Migrating immune cells globally coordinate protrusive forces}},
  doi          = {10.1038/s41590-025-02211-w},
  volume       = {26},
  year         = {2025},
}

@article{17279,
  abstract     = {In a recent issue of Cell, Zhang et al.1 demonstrate that mechanical features of a solid tumor can drive T cells into dysfunctionality and identify pathways that revert this “exhausted” state.},
  author       = {Avellaneda Sarrió, Mario and Sixt, Michael K},
  issn         = {2451-9448},
  journal      = {Cell Chemical Biology},
  number       = {7},
  pages        = {1242--1243},
  publisher    = {Elsevier},
  title        = {{Rescuing T cells from stiff tumors}},
  doi          = {10.1016/j.chembiol.2024.06.011},
  volume       = {31},
  year         = {2024},
}

@inbook{14848,
  abstract     = {Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.},
  author       = {Wruck, F. and Avellaneda Sarrió, Mario and Naqvi, M. M. and Koers, E. J. and Till, K. and Gross, L. and Moayed, F. and Roland, A. and Heling, L. W. H. J. and Mashaghi, A. and Tans, S. J.},
  booktitle    = {Biophysics of Molecular Chaperones},
  editor       = {Hiller, Sebastian and Liu, Maili and He, Lichun},
  isbn         = {9781839162824},
  pages        = {278--318},
  publisher    = {Royal Society of Chemistry},
  title        = {{Probing Single Chaperone Substrates}},
  doi          = {10.1039/bk9781839165986-00278},
  volume       = {29},
  year         = {2023},
}

@article{12085,
  abstract     = {Molecular catch bonds are ubiquitous in biology and essential for processes like leucocyte extravasion1 and cellular mechanosensing2. Unlike normal (slip) bonds, catch bonds strengthen under tension. The current paradigm is that this feature provides ‘strength on demand3’, thus enabling cells to increase rigidity under stress1,4,5,6. However, catch bonds are often weaker than slip bonds because they have cryptic binding sites that are usually buried7,8. Here we show that catch bonds render reconstituted cytoskeletal actin networks stronger than slip bonds, even though the individual bonds are weaker. Simulations show that slip bonds remain trapped in stress-free areas, whereas weak binding allows catch bonds to mitigate crack initiation by moving to high-tension areas. This ‘dissociation on demand’ explains how cells combine mechanical strength with the adaptability required for shape change, and is relevant to diseases where catch bonding is compromised7,9, including focal segmental glomerulosclerosis10 caused by the α-actinin-4 mutant studied here. We surmise that catch bonds are the key to create life-like materials.},
  author       = {Mulla, Yuval and Avellaneda Sarrió, Mario and Roland, Antoine and Baldauf, Lucia and Jung, Wonyeong and Kim, Taeyoon and Tans, Sander J. and Koenderink, Gijsje H.},
  issn         = {1476-4660},
  journal      = {Nature Materials},
  number       = {9},
  pages        = {1019--1023},
  publisher    = {Springer Nature},
  title        = {{Weak catch bonds make strong networks}},
  doi          = {10.1038/s41563-022-01288-0},
  volume       = {21},
  year         = {2022},
}

@article{17072,
  abstract     = {The collapse of polypeptides is thought important to protein folding, aggregation, intrinsic disorder, and phase separation. However, whether polypeptide collapse is modulated in cells to control protein states is unclear. Here, using integrated protein manipulation and imaging, we show that the chaperonin GroEL-ES can accelerate the folding of proteins by strengthening their collapse. GroEL induces contractile forces in substrate chains, which draws them into the cavity and triggers a general compaction and discrete folding transitions, even for slow-folding proteins. This collapse enhancement is strongest in the nucleotide-bound states of GroEL and is aided by GroES binding to the cavity rim and by the amphiphilic C-terminal tails at the cavity bottom. Collapse modulation is distinct from other proposed GroEL-ES folding acceleration mechanisms, including steric confinement and misfold unfolding. Given the prevalence of collapse throughout the proteome, we conjecture that collapse modulation is more generally relevant within the protein quality control machinery.},
  author       = {Naqvi, Mohsin M. and Avellaneda Sarrió, Mario and Roth, Andrew and Koers, Eline J. and Roland, Antoine and Sunderlikova, Vanda and Kramer, Günter and Rye, Hays S. and Tans, Sander J.},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {9},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Protein chain collapse modulation and folding stimulation by GroEL-ES}},
  doi          = {10.1126/sciadv.abl6293},
  volume       = {8},
  year         = {2022},
}