WIPF1

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Protein-coding gene in the species Homo sapiens

title: "WIPF1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["evh1-domain"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/evh1-domain" source: "https://en.wikipedia.org/wiki/WIPF1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.

Function

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. 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. In patients lacking the WIPF1 gene WASp protein levels are depleted and WAS symptoms present.

Interactions

WIP has been shown to interact with Wiskott–Aldrich syndrome protein, N-WASp, Cortactin, NCK1, and ITSN1. While Wiskott–Aldrich syndrome protein (WASp)is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously. The majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp. These mutations affect WASp-WIPF1 binding. 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

WIPF1 functions and interactions have been studied in multiple fungal systems including Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans, and Magnaporthe grisea.

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. In addition to a role in endocytosis, Saccharomyces cerevisiae Vrp1 functions in cytokinesis and cell polarization.

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.

References

References

  1. (December 1997). "WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells". Proceedings of the National Academy of Sciences of the United States of America.
  2. "Entrez Gene: WIPF1 WAS/WASL interacting protein family, member 1".
  3. (January 2012). "A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP". The Journal of Experimental Medicine.
  4. (August 1998). "The Wiskott–Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". The Journal of Biological Chemistry.
  5. (March 2003). "Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion". Current Biology.
  6. (August 2012). "Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis". Molecular Biology of the Cell.
  7. (July 2015). "Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia". Cellular Signalling.
  8. (December 2009). "Characterization of Wiskott–Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae". FEMS Yeast Research.
  9. (April 2006). "WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP". Biochemical and Biophysical Research Communications.
  10. Borth, Nicole. (July 19, 2010). "Candida albicans Vrp1 is required for polarized morphogenesis and interacts with Wal1 and Myo5". Microbiology.
  11. Huang, Lin. (January 24, 2017). "MoVrp1, a putative verprolin protein, is required for asexual development and infection in the rice blast fungus Magnaporthe oryzae". Scientific Reports.
  12. (2005-08-15). "Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast". The Journal of Cell Biology.
  13. (July 2009). "Verprolin: a cool set of actin-binding sites and some very HOT prolines". IUBMB Life.
  14. (September 2019). "S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly". Journal of Cell Science.

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