Gunning, P. W., Ghoshdastider, U., Whitaker, S., Popp, D. & Robinson, R. C. The evolution of compositionally and functionally distinct actin filaments. J. Cell Sci. 128, 2009–2019 (2015).
CAS PubMed Article Google Scholar
Akıl, C. et al. Mythical origins of the actin cytoskeleton. Curr. Opin. Cell Biol. 68, 55–63 (2021).
PubMed Article CAS Google Scholar
Pollard, T. D. Actin and actin-binding proteins. Cold Spring Harb. Perspect. Biol. 8, a018226 (2016).
PubMed PubMed Central Article CAS Google Scholar
Oda, T., Iwasa, M., Aihara, T., Maéda, Y. & Narita, A. The nature of the globular- to fibrous-actin transition. Nature 457, 441–445 (2009).
CAS PubMed Article Google Scholar
Merino, F. et al. Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. Nat. Struct. Mol. Biol. 25, 528–537 (2018).
CAS PubMed Article Google Scholar
Chou, S. Z. & Pollard, T. D. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. Proc. Natl Acad. Sci. USA 116, 4265–4274 (2019).
CAS PubMed PubMed Central Article Google Scholar
Pollard, T. D. & Cooper, J. A. Actin, a central player in cell shape and movement. Science 326, 1208–1212 (2009).
CAS PubMed PubMed Central Article Google Scholar
Blanchoin, L., Boujemaa-Paterski, R., Sykes, C. & Plastino, J. Actin dynamics, architecture, and mechanics in cell motility. Physiol. Rev. 94, 235–263 (2014).
CAS PubMed Article Google Scholar
Livne, A. & Geiger, B. The inner workings of stress fibers − from contractile machinery to focal adhesions and back. J. Cell Sci. 129, 1293–1304 (2016).
CAS PubMed Article Google Scholar
Anderson, C. A., Kovar, D. R., Gardel, M. L. & Winkelman, J. D. LIM domain proteins in cell mechanobiology. Cytoskeleton 78, 303–311 (2021).
CAS PubMed Article Google Scholar
Mogilner, A. & Oster, G. Polymer motors: pushing out the front and pulling up the back. Curr. Biol. 13, R721–R733 (2003).
CAS PubMed Article Google Scholar
Kaksonen, M., Sun, Y. & Drubin, D. G. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115, 475–487 (2003).
CAS PubMed Article Google Scholar
Lacy, M. M., Baddeley, D. & Berro, J. Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis. Elife 8, e52355 (2019).
CAS PubMed PubMed Central Article Google Scholar
Lai, F. P. et al. Arp2/3 complex interactions and actin network turnover in lamellipodia. EMBO J. 27, 982–992 (2008).
CAS PubMed PubMed Central Article Google Scholar
Sept, D. & McCammon, J. A. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81, 667–674 (2001).
CAS PubMed PubMed Central Article Google Scholar
Funk, J. et al. Profilin and formin constitute a pacemaker system for robust actin filament growth. Elife 8, e50963 (2019).
CAS PubMed PubMed Central Article Google Scholar
Xue, B. & Robinson, R. C. Guardians of the actin monomer. Eur. J. Cell Biol. 92, 316–332 (2013).
CAS PubMed Article Google Scholar
Koestler, S. A. et al. F- and G-actin concentrations in lamellipodia of moving cells. PLoS ONE 4, e4810 (2009).
PubMed PubMed Central Article CAS Google Scholar
Boujemaa-Paterski, R. et al. Network heterogeneity regulates steering in actin-based motility. Nat. Commun. 8, 655 (2017).
PubMed PubMed Central Article CAS Google Scholar
Malik-Garbi, M. et al. Scaling behaviour in steady-state contracting actomyosin networks. Nat. Phys. 15, 509–516 (2019).
CAS PubMed PubMed Central Article Google Scholar
Rodriguez, A. J., Shenoy, S. M., Singer, R. H. & Condeelis, J. Visualization of mRNA translation in living cells. J. Cell Biol. 175, 67–76 (2006).
CAS PubMed PubMed Central Article Google Scholar
Safer, D., Golla, R. & Nachmias, V. T. Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets. Proc. Natl Acad. Sci. USA 87, 2536–2540 (1990).
CAS PubMed PubMed Central Article Google Scholar
Pollard, T. D. & Cooper, J. A. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23, 6631–6641 (1984).
CAS PubMed Article Google Scholar
Gautreau, A. M., Fregoso, F. E., Simanov, G. & Dominguez, R. Nucleation, stabilization, and disassembly of branched actin networks. Trends Cell Biol. 32, 421–432 (2022).
CAS PubMed Article Google Scholar
Machesky, L. M. et al. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA 96, 3739–3744 (1999).
CAS PubMed PubMed Central Article Google Scholar
Bieling, P. et al. WH2 and proline-rich domains of WASP-family proteins collaborate to accelerate actin filament elongation. EMBO J. 37, 102–121 (2018). This article describes how polyproline sequences of WASP family proteins support filament elongation by bringing assembly-competent profilin–actin complexes to filament barbed ends, and also by transferring actin monomers to the nearby WH2 domains of the NPFs. Also, unoccupied WH2 domains potently tether actin network to membranes.
CAS PubMed Article Google Scholar
Padrick, S. B., Doolittle, L. K., Brautigam, C. A., King, D. S. & Rosen, M. K. Arp2/3 complex is bound and activated by two WASP proteins. Proc. Natl Acad. Sci. USA 108, E472–E479 (2011).
CAS PubMed PubMed Central Article Google Scholar
Ti, S.-C., Jurgenson, C. T., Nolen, B. J. & Pollard, T. D. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc. Natl Acad. Sci. USA 108, E463–E471 (2011).
CAS PubMed PubMed Central Article Google Scholar
Zimmet, A. et al. Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism. Sci. Adv. 6, eaaz7651 (2020).
CAS PubMed PubMed Central Article Google Scholar
Shaaban, M., Chowdhury, S. & Nolen, B. J. Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state. Nat. Struct. Mol. Biol. 27, 1009–1016 (2020).
CAS PubMed PubMed Central Article Google Scholar
Blanchoin, L. et al. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007–1011 (2000).
CAS PubMed Article Google Scholar
Smith, B. A. et al. Three-color single molecule imaging shows WASP detachment from Arp2/3 complex triggers actin filament branch formation. Elife 2, e01008 (2013).
PubMed PubMed Central Article Google Scholar
Svitkina, T. M. & Borisy, G. G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009–1026 (1999).
CAS PubMed PubMed Central Article Google Scholar
Mullins, R. D., Heuser, J. A. & Pollard, T. D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl Acad. Sci. USA 95, 6181–6186 (1998).
CAS PubMed PubMed Central Article Google Scholar
Kovar, D. R. & Pollard, T. D. Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl Acad. Sci. USA 101, 14725–14730 (2004).
CAS PubMed PubMed Central Article Google Scholar
Romero, S. et al. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419–429 (2004).
CAS PubMed Article Google Scholar
Courtemanche, N. Mechanisms of formin-mediated actin assembly and dynamics. Biophys. Rev. 10, 1553–1569 (2018).
留言 (0)