WH2 motif
| WH2 motif | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| Symbol | WH2 | ||||||||
| Pfam | PF02205 | ||||||||
| InterPro | IPR003124 | ||||||||
| SMART | WH2 | ||||||||
| SCOP | 1ej5 | ||||||||
| SUPERFAMILY | 1ej5 | ||||||||
| |||||||||
Function
The WH2 motif or WH2 domain is an evolutionarily conserved sequence motif contained in proteins.[2] It is found in WASP proteins which control actin polymerisation, therefore, WH2 is important in cellular processes such as cell contractility, cell motility, cell trafficking and cell signalling.[3]
Motif
The WH2 motif (for Wiskott-Aldrich syndrome homology region 2) has been shown in WAS and Scar1/WASF1 (mammalian homologue) to interact via their WH2 motifs with actin.
The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognized as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds to actin monomers and can facilitate the assembly of actin monomers into actin filaments.[4][5]
Examples
Human genes encoding proteins containing the WH2 motif include:
- COBL, COBLL1, ESPN, INF2, JMY
- LMOD1, LMOD2, LMOD3
- MTSS1, PXK
- WAS, WASF1, WASF2, WASF3, WASF4, WASL, WASPIP, WHDC1, WIPF1, WIPF2
References
- ↑ PDB: 2d1k; Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R (February 2007). "Structural basis for the actin-binding function of missing-in-metastasis". Structure. 15 (2): 145–55. doi:10.1016/j.str.2006.12.005. PMC 1853380
. PMID 17292833. - ↑ Machesky LM, Insall RH (1998). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Curr. Biol. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097.
- ↑ Veltman DM, Insall RH (2010). "WASP family proteins: their evolution and its physiological implications.". Mol Biol Cell. 21 (16): 2880–93. doi:10.1091/mbc.E10-04-0372. PMC 2921111. PMID 20573979.
- ↑ Machesky LM, Insall RH, Volkman LE (2001). "WASP homology sequences in baculoviruses". Trends Cell Biol. 11 (7): 286–287. doi:10.1016/S0962-8924(01)02009-8. PMID 11434350.
- ↑ Lappalainen P, Paunola E, Mattila PK (2002). "WH2 domain: a small, versatile adapter for actin monomers". FEBS Lett. 513 (1): 92–97. doi:10.1016/S0014-5793(01)03242-2. PMID 11911886.
This article incorporates text from the public domain Pfam and InterPro IPR003124