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WIPF1

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WIPF1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesWIPF1, PRPL-2, WASPIP, WIP, WAS2, WAS/WASL interacting protein family member 1
External IDsOMIM: 602357; MGI: 2178801; HomoloGene: 86891; GeneCards: WIPF1; OMA:WIPF1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

7456

215280

Ensembl

ENSG00000115935

ENSMUSG00000075284

UniProt

O43516

Q8K1I7

RefSeq (mRNA)

NM_001077269
NM_003387

NM_001289722
NM_001289723
NM_153138

RefSeq (protein)

NP_001276651
NP_001276652
NP_694778

Location (UCSC)Chr 2: 174.56 – 174.68 MbChr 2: 73.26 – 73.36 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.[5][6]

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.[5] 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.[6] In patients lacking the WIPF1 gene WASp protein levels are depleted and WAS symptoms present.[7]

Interactions

WIP has been shown to interact with Wiskott–Aldrich syndrome protein,[5][8] N-WASp, Cortactin,[9] NCK1,[8] MYO1e[10] and ITSN1.[11] While Wiskott–Aldrich syndrome protein (WASp)is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously.[5] The majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp.[12] These mutations affect WASp-WIPF1 binding.[13] 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,[14] and Magnaporthe grisea.[15]

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.[16] In addition to a role in endocytosis, Saccharomyces cerevisiae Vrp1 functions in cytokinesis and cell polarization.[17]

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.[18]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115935 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000075284 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d Ramesh N, Antón IM, Hartwig JH, Geha RS (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. 94 (26): 14671–6. Bibcode:1997PNAS...9414671R. doi:10.1073/pnas.94.26.14671. PMC 25088. PMID 9405671.
  6. ^ a b "Entrez Gene: WIPF1 WAS/WASL interacting protein family, member 1".
  7. ^ Lanzi G, Moratto D, Vairo D, Masneri S, Delmonte O, Paganini T, et al. (January 2012). "A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP". The Journal of Experimental Medicine. 209 (1): 29–34. doi:10.1084/JEM.20110896. hdl:11379/487873. PMC 3260865. PMID 22231303.
  8. ^ a b Antón IM, Lu W, Mayer BJ, Ramesh N, Geha RS (August 1998). "The Wiskott–Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". The Journal of Biological Chemistry. 273 (33): 20992–5. doi:10.1074/jbc.273.33.20992. PMID 9694849.
  9. ^ Kinley AW, Weed SA, Weaver AM, Karginov AV, Bissonette E, Cooper JA, Parsons JT (March 2003). "Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion". Current Biology. 13 (5): 384–93. doi:10.1016/S0960-9822(03)00107-6. PMID 12620186. S2CID 17357571.
  10. ^ Cheng J, Grassart A, Drubin DG (August 2012). "Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis". Molecular Biology of the Cell. 23 (15): 2891–904. doi:10.1091/mbc.e11-04-0383. PMC 3408416. PMID 22675027.
  11. ^ Gryaznova T, Kropyvko S, Burdyniuk M, Gubar O, Kryklyva V, Tsyba L, Rynditch A (July 2015). "Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia". Cellular Signalling. 27 (7): 1499–508. doi:10.1016/j.cellsig.2015.03.006. PMID 25797047.
  12. ^ Rajmohan R, Raodah A, Wong MH, Thanabalu T (December 2009). "Characterization of Wiskott–Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae". FEMS Yeast Research. 9 (8): 1226–35. doi:10.1111/j.1567-1364.2009.00581.x. PMID 19817875.
  13. ^ Rajmohan R, Meng L, Yu S, Thanabalu T (April 2006). "WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP". Biochemical and Biophysical Research Communications. 342 (2): 529–36. doi:10.1016/j.bbrc.2006.01.160. PMID 16488394.
  14. ^ Borth, Nicole (July 19, 2010). "Candida albicans Vrp1 is required for polarized morphogenesis and interacts with Wal1 and Myo5" (PDF). Microbiology. 156 (Pt 10): 2962–2969. doi:10.1099/mic.0.041707-0. PMID 20656786.
  15. ^ 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. Bibcode:2017NatSR...741148H. doi:10.1038/srep41148. PMC 5259722. PMID 28117435.
  16. ^ 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. PMC 2171502. PMID 16087707.
  17. ^ 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. hdl:10072/30097. ISSN 1521-6551. PMID 19507265. S2CID 6788285.
  18. ^ MacQuarrie CD, Mangione MC, Carroll R, James M, Gould KL, Sirotkin V (September 2019). "S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly". Journal of Cell Science. 132 (17): jcs233502. doi:10.1242/jcs.233502. PMC 6771142. PMID 31391237.

Further reading

  • 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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