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WAS/WASL-interacting protein family member 1 (WIP) is a protein that in humans is encoded by the WIPF1 gene.[1][2]
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]
WIPF1 has been shown to interact with Wiskott-Aldrich syndrome protein,[1][4] Cortactin[5], NCK1[4], and ITSN1[6]. While Wiskott-Aldrich syndrome protein is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously[1]. Majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp.[7] These mutations affect WASp-WIPF1 binding.[8] WIPF1 yeast homologue verprolin Vrp1 binds class 1 myosin and enhances class 1 myosin dependent actin nucleation.[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.