WIPF1
Lua error in Module:Infobox_gene at line 53: attempt to index field 'wikibase' (a nil value). WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.[1][2]
Function
[edit | edit source]This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. Overexpression of WIP in mammalian cells has been shown to increase actin polymerization.[1] The encoded protein binds to a region of Wiskott–Aldrich syndrome protein that is frequently mutated in Wiskott–Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene.[2] In patients lacking the WIPF1 gene WASp protein levels are depleted and WAS symptoms present.[3]
Interactions
[edit | edit source]WIP has been shown to interact with Wiskott–Aldrich syndrome protein,[1][4] N-WASp, Cortactin,[5] NCK1,[4] MYO1e[6] and ITSN1.[7] While Wiskott–Aldrich syndrome protein (WASp)is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously.[1] The majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp.[8] These mutations affect WASp-WIPF1 binding.[9] WIPF1 has an N-terminal profilin binding domain, two actin binding WH2 domains, a central polyproline stretch, and a C-terminal WASp Binding Domain. WASp protein is degraded in the absence of WIP; but the ubiquitously expressed WASp ortholog N-WASp remains stable in the absence of WIP.
Work in yeast
[edit | edit source]WIPF1 functions and interactions have been studied in multiple fungal systems including Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans,[10] and Magnaporthe grisea.[11]
Yeast Vrp1 is recruited to sites of endocytosis by WASp homologs. Here it interacts with myosin-1 and enhances myosin-1 mediated activation of the Arp2/3 complex.[12] In addition to a role in endocytosis, Saccharomyces cerevisiae Vrp1 functions in cytokinesis and cell polarization.[13]
In Schizosaccharomyces pombe, Vrp1 interaction with myosin-1 is believed to help position new actin branches near the membrane, enhancing the amount of force against the membrane. This interaction is disrupted by the yeast specific protein Bbc1/Mti1/SPAC23A1.17, which competes with Vrp1 for binding the Myo1e homolog.[14]
References
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Further reading
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