WASL (gene)

From Wikipedia, the free encyclopedia

Wiskott-Aldrich syndrome-like

Identifiers

WASL; DKFZp779G0847; MGC48327; N-WASP

External IDs

OMIM: 605056 MGI: 1920428 HomoloGene: 74515

Gene ontology
Molecular Function:	• actin binding • small GTPase regulator activity • protein binding
Cellular Component:	• nucleus • actin cytoskeleton • lamellipodium
Biological Process:	• transcription • regulation of transcription, DNA-dependent • protein complex assembly • cell motility • actin polymerization and/or depolymerization • response to bacterium

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003941 (mRNA)
NP_003932 (protein)

NM_028459 (mRNA)
NP_082735 (protein)

Location

Chr 7: 123.11 - 123.18 Mb

Chr 6: 24.56 - 24.61 Mb

Pubmed search

[1]

[2]

Wiskott-Aldrich syndrome-like, also known as WASL, is a human gene.^[1]

The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3. The WASL gene product is a homolog of WAS protein, however, unlike the latter, it is ubiquitously expressed and shows highest expression in neural tissues. It has been shown to bind Cdc42 directly, and induce formation of long actin microspikes.^[1]

[edit] References

^ ^a ^b Entrez Gene: WASL Wiskott-Aldrich syndrome-like.

[edit] Further reading

Ramesh N, Antón IM, Martínez-Quiles N, Geha RS (1999). "Waltzing with WASP.". Trends Cell Biol. 9 (1): 15–9. PMID 10087612.
Carlier MF, Ducruix A, Pantaloni D (1999). "Signalling to actin: the Cdc42-N-WASP-Arp2/3 connection.". Chem. Biol. 6 (9): R235–40. PMID 10467124.
Fukuoka M, Miki H, Takenawa T (1997). "Identification of N-WASP homologs in human and rat brain.". Gene 196 (1-2): 43–8. PMID 9322739.
Miki H, Sasaki T, Takai Y, Takenawa T (1998). "Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP.". Nature 391 (6662): 93–6. doi:10.1038/34208. PMID 9422512.
Suzuki T, Miki H, Takenawa T, Sasakawa C (1998). "Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri.". EMBO J. 17 (10): 2767–76. doi:10.1093/emboj/17.10.2767. PMID 9582270.
Suetsugu S, Miki H, Takenawa T (1999). "The essential role of profilin in the assembly of actin for microspike formation.". EMBO J. 17 (22): 6516–26. doi:10.1093/emboj/17.22.6516. PMID 9822597.
Qualmann B, Roos J, DiGregorio PJ, Kelly RB (1999). "Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein.". Mol. Biol. Cell 10 (2): 501–13. PMID 9950691.
Suetsugu S, Miki H, Takenawa T (1999). "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex.". Biochem. Biophys. Res. Commun. 260 (1): 296–302. doi:10.1006/bbrc.1999.0894. PMID 10381382.
Egile C, Loisel TP, Laurent V, et al. (1999). "Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility.". J. Cell Biol. 146 (6): 1319–32. PMID 10491394.
Higgs HN, Blanchoin L, Pollard TD (1999). "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization.". Biochemistry 38 (46): 15212–22. PMID 10563804.
Qualmann B, Kelly RB (2000). "Syndapin isoforms participate in receptor-mediated endocytosis and actin organization.". J. Cell Biol. 148 (5): 1047–62. PMID 10704453.
Kim AS, Kakalis LT, Abdul-Manan N, et al. (2000). "Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.". Nature 404 (6774): 151–8. doi:10.1038/35004513. PMID 10724160.
Carlier MF, Nioche P, Broutin-L'Hermite I, et al. (2000). "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex.". J. Biol. Chem. 275 (29): 21946–52. doi:10.1074/jbc.M000687200. PMID 10781580.
Mimuro H, Suzuki T, Suetsugu S, et al. (2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri.". J. Biol. Chem. 275 (37): 28893–901. doi:10.1074/jbc.M003882200. PMID 10867004.
Prehoda KE, Scott JA, Mullins RD, Lim WA (2000). "Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex.". Science 290 (5492): 801–6. PMID 11052943.
Modregger J, Ritter B, Witter B, et al. (2001). "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis.". J. Cell. Sci. 113 Pt 24: 4511–21. PMID 11082044.
Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex.". Nat. Cell Biol. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629.
Fukuoka M, Suetsugu S, Miki H, et al. (2001). "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42.". J. Cell Biol. 152 (3): 471–82. PMID 11157975.