The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Regulation of Actin Filament Network Formation Through ARP2/3 Complex: Activation by a Diverse Array of Proteins
Abstract
▪ Abstract Actin filament assembly and turnover drive many forms of cellular motility, particularly extension of the leading edge of locomoting cells and rocketing of pathogenic microorganisms through host cell cytoplasm. De novo nucleation of actin filaments appears to be required for these movements. A complex of seven proteins called Arp2/3 complex is the best characterized cellular initiator of actin filament nucleation. Arp2/3 complex is intrinsically inactive, relying on nucleation promoting factors for activation. WASp/Scar family proteins are prominent cellular nucleation promoting factors. They bring together an actin monomer and Arp2/3 complex in solution or on the side of an existing actin filament to initiate a new filament that grows in the barbed end direction. WASp and N-WASP are intrinsically autoinhibited, and their activity is regulated by Rho-family GTPases such as Cdc42, membrane polyphosphoinositides, WIP/verprolin, and SH3 domain proteins. These interactions provide a final common pathway for many signaling inputs to regulate actin polymerization. Microorganisms either activate Arp2/3 complex directly or usurp N-WASP to initiate actin polymerization.
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Citations
Cites
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773
Self-citationBlanchoin, L., Amann, K. J., Higgs, H. N., Marchand, J.-B., Kaiser, D. A., & Pollard, T. D. (2000) · Nature · doi:10.1038/35010008 · Cited by 586
Self-citationInteraction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
Marchand, J.-B., Kaiser, D. A., Pollard, T. D., & Higgs, H. N. (2001) · Nature Cell Biology · doi:10.1038/35050590 · Cited by 331
Self-citationSuetsugu, S., Miki, H., & Takenawa, T. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0894 · Cited by 246
Cited by
Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A.-C., Bösche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A.-M., Cruciat, C.-M., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,759
Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M., & Kirschner, M. W. (2002) · Nature · doi:10.1038/nature00859 · Cited by 835
The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
Linder, S. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.01.002 · Cited by 640
Crystal Structure of Arp2/3 Complex
Robinson, R. C., Turbedsky, K., Kaiser, D. A., Marchand, J.-B., Higgs, H. N., Choe, S., & Pollard, T. D. (2001) · Science · doi:10.1126/science.1066333 · Cited by 540
Self-citationNiessen, C. M., Leckband, D., & Yap, A. S. (2011) · Physiological Reviews · doi:10.1152/physrev.00004.2010 · Cited by 427
Metadata
- Authors
- Higgs, H. N., & Pollard, T. D.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2001-06
- Volume
- 70
- Issue
- 1
- Pages
- 649-676
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2110726109
- Cited by
- 673
- References
- 4
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
