Biology:WIPF1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.[1][2]

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.[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

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

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

  1. ↑ 1.0 1.1 1.2 1.3 "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 94 (26): 14671–6. December 1997. doi:10.1073/pnas.94.26.14671. PMID 9405671. Bibcode: 1997PNAS...9414671R. 
  2. ↑ 2.0 2.1 "Entrez Gene: WIPF1 WAS/WASL interacting protein family, member 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7456. 
  3. ↑ "A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP". The Journal of Experimental Medicine 209 (1): 29–34. January 2012. doi:10.1084/JEM.20110896. PMID 22231303. 
  4. ↑ 4.0 4.1 "The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". The Journal of Biological Chemistry 273 (33): 20992–5. August 1998. doi:10.1074/jbc.273.33.20992. PMID 9694849. 
  5. ↑ "Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion". Current Biology 13 (5): 384–93. March 2003. doi:10.1016/S0960-9822(03)00107-6. PMID 12620186. 
  6. ↑ "Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis". Molecular Biology of the Cell 23 (15): 2891–904. August 2012. doi:10.1091/mbc.e11-04-0383. PMID 22675027. 
  7. ↑ "Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia". Cellular Signalling 27 (7): 1499–508. July 2015. doi:10.1016/j.cellsig.2015.03.006. PMID 25797047. 
  8. ↑ "Characterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae". FEMS Yeast Research 9 (8): 1226–35. December 2009. doi:10.1111/j.1567-1364.2009.00581.x. PMID 19817875. 
  9. ↑ "WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP". Biochemical and Biophysical Research Communications 342 (2): 529–36. April 2006. doi:10.1016/j.bbrc.2006.01.160. PMID 16488394. 
  10. ↑ Borth, Nicole (July 19, 2010). "Candida albicans Vrp1 is required for polarized morphogenesis and interacts with Wal1 and Myo5". Microbiology 156 (Pt 10): 2962–2969. doi:10.1099/mic.0.041707-0. PMID 20656786. https://www.microbiologyresearch.org/docserver/fulltext/micro/156/10/2962.pdf?expires=1569465631&id=id&accname=guest&checksum=AC93FFD82242829954207D5FDFF2BEA0. 
  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 7: 41148. doi:10.1038/srep41148. PMID 28117435. Bibcode: 2017NatSR...741148H. 
  12. ↑ Sirotkin, Vladimir; Beltzner, Christopher C.; Marchand, Jean-Baptiste; Pollard, Thomas D. (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 170 (4): 637–648. doi:10.1083/jcb.200502053. ISSN 0021-9525. PMID 16087707. 
  13. ↑ Munn, Alan L.; Thanabalu, Thirumaran (July 2009). "Verprolin: a cool set of actin-binding sites and some very HOT prolines". IUBMB Life 61 (7): 707–712. doi:10.1002/iub.195. ISSN 1521-6551. PMID 19507265. 
  14. ↑ "S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly". Journal of Cell Science 132 (17): jcs233502. September 2019. doi:10.1242/jcs.233502. PMID 31391237. 

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: O43516 (WAS/WASL-interacting protein family member 1) at the PDBe-KB.




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