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The Wiskott–Aldrich Syndrome protein (WASp) is a 502-amino acid protein expressed in cells of the hematopoietic system that in humans is encoded by the WAS gene. In the inactive state, WASp exists in an autoinhibited conformation with sequences near its C-terminus binding to a region near its N-terminus. Its activation is dependent upon CDC42 and PIP2 acting to disrupt this interaction, causing the WASp protein to 'open'. This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex. Activated Arp2/3 nucleates new F-actin.
The lamellipodium is a cytoskeletal protein actin projection on the leading edge of the cell. It contains a quasi-two-dimensional actin mesh; the whole structure propels the cell across a substrate. Within the lamellipodia are ribs of actin called microspikes, which, when they spread beyond the lamellipodium frontier, are called filopodia. The lamellipodium is born of actin nucleation in the plasma membrane of the cell and is the primary area of actin incorporation or microfilament formation of the cell.
ADF/cofilin is a family of actin-binding proteins which disassembles actin filaments. Three highly conserved and highly (70%-82%) identical genes belonging to this family have been described in humans and mice:
Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.
Cofilin 1 , also known as CFL1, is a human gene, part of the ADF/cofilin family.
Cortactin is a monomeric protein located in the cytoplasm of cells that can be activated by external stimuli to promote polymerization and rearrangement of the actin cytoskeleton, especially the actin cortex around the cellular periphery. It is present in all cell types. When activated, it will recruit Arp2/3 complex proteins to existing actin microfilaments, facilitating and stabilizing nucleation sites for actin branching. Cortactin is important in promoting lamellipodia formation, invadopodia formation, cell migration, and endocytosis.
LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.
Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.
Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.
Fascin is a protein that in humans is encoded by the FSCN1 gene.
Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene.
Protein enabled homolog is a protein that in humans is encoded by the ENAH gene.
Actin-related protein 2/3 complex subunit 2 is a protein that in humans is encoded by the ARPC2 gene.
For the SSH-1 protocol, see Secure Shell#Version 1.x
Coronin-1C is a protein that in humans is encoded by the CORO1C gene.
For the SSH-2 protocol, see Secure Shell#Version 2.x
Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis. Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to humans.
Protein phosphatase Slingshot homolog 3 is an enzyme that in humans is encoded by the SSH3 gene.
Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.
Coronin, actin binding protein, 2A is a protein that in humans is encoded by the CORO2A gene.
References
- ↑ Okumura M, Kung C, Wong S, Rodgers M, Thomas ML (September 1998). "Definition of family of coronin-related proteins conserved between humans and mice: close genetic linkage between coronin-2 and CD45-associated protein". DNA Cell Biol. 17 (9): 779–87. doi:10.1089/dna.1998.17.779. PMID 9778037.
- 1 2 Cai L, Holoweckyj N, Schaller MD, Bear JE (September 2005). "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility". J. Biol. Chem. 280 (36): 31913–23. doi: 10.1074/jbc.M504146200 . PMID 16027158.
- ↑ "Entrez Gene: CORO1B coronin, actin binding protein, 1B".
- ↑ Cai L, Makhov AM, Schafer DA, Bear JE (September 2008). "Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia". Cell. 134 (5): 828–42. doi:10.1016/j.cell.2008.06.054. PMC 2570342 . PMID 18775315.
- ↑ Cai L, Makhov AM, Bear JE (May 2007). "F-actin binding is essential for coronin 1B function in vivo". J. Cell Sci. 120 (Pt 10): 1779–90. doi: 10.1242/jcs.007641 . PMID 17456547.
- ↑ Cai L, Marshall TW, Uetrecht AC, Schafer DA, Bear JE (March 2007). "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge". Cell. 128 (5): 915–29. doi:10.1016/j.cell.2007.01.031. PMC 2630706 . PMID 17350576.
- ↑ Di Giovanni S, De Biase A, Yakovlev A, Finn T, Beers J, Hoffman EP, Faden AI (January 2005). "In vivo and in vitro characterization of novel neuronal plasticity factors identified following spinal cord injury". J. Biol. Chem. 280 (3): 2084–91. doi: 10.1074/jbc.M411975200 . PMID 15522871.
- ↑ Parente JA, Chen X, Zhou C, Petropoulos AC, Chew CS (January 1999). "Isolation, cloning, and characterization of a new mammalian coronin family member, coroninse, which is regulated within the protein kinase C signaling pathway". J. Biol. Chem. 274 (5): 3017–25. doi: 10.1074/jbc.274.5.3017 . PMID 9915840.
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