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Gene Review

WIPF1  -  WAS/WASL interacting protein family, member 1

Homo sapiens

Synonyms: PRPL-2, Protein PRPL-2, WAS/WASL-interacting protein family member 1, WASP-interacting protein, WASPIP, ...
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Disease relevance of WIPF1

  • Our previous studies have shown that N-WASP is required for the actin-based motility of vaccinia virus and is recruited via Nck and WIP [1].
  • We have now identified and characterized the N-WASP WH1 binding motif in WIP in vitro and in vivo using Shigella and vaccinia systems [2].
  • Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome [3].
  • National guidelines for the prevention of hospital infections in The Netherlands were established by the Working Group on Infection Prevention (WIP) in 1981 [4].

Psychiatry related information on WIPF1

  • Conditional uncertainty analysis and implications for decision making: the case of WIPP [5].

High impact information on WIPF1

  • These results suggest that WIP is important for immunologic synapse formation and T cell activation [6].
  • WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation [6].
  • In contrast, WIP-deficient B lymphocytes have enhanced proliferation and CD69 expression following B cell receptor ligation and mount normal antibody responses to T-independent antigens [6].
  • WIP stabilizes actin filaments and is important for filopodium formation [6].
  • In this review, the authors discuss the possible role of WASP/NWASP and of the newly described protein WIP, which interacts with WASP and NWASP, in coupling signals from the T-cell receptor to the actin-based cytoskeleton [7].

Biological context of WIPF1


Anatomical context of WIPF1

  • By using the yeast two-hybrid system we have identified a proline-rich WASP-interacting protein (WIP), which coimmunoprecipitated with WASP from lymphocytes [12].
  • CONCLUSIONS: WIP, a protein involved in filopodia formation, binds to both actin monomers and cortactin [9].
  • Furthermore, WIP-knockdown experiments demonstrated that T cells with reduced WIP expression show a concordant reduction of WASP levels [13].
  • Here we show that WASP gene transfer results in high WASP expression only when WIP is concomitantly expressed in K562 cells [13].
  • Thus, the multiprotein complex is important for NK cell function, killer cell immunoglobulin-like receptor inhibitory signaling affects proteins involved in cytoskeletal rearrangements, and WIP plays a central role in the formation of the complex and in the regulation of NK cell activity [14].

Associations of WIPF1 with chemical compounds


Physical interactions of WIPF1


Other interactions of WIPF1

  • Lastly, coexpression of cortactin and WIP stimulated membrane protrusions [9].
  • A role for WIP in cell polarity provides a framework for unifying, under a common paradigm, distinct molecular defects associated with immunodeficiencies like Wiskott-Aldrich syndrome [8].
  • Our clone of this protein, termed WASP interacting protein (WIP) by others, shows a difference in seven amino acid residues, compared with the previously published sequence revealing an additional profilin binding motif [19].
  • Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1 [20].
  • This report presents a novel WIP-like protein, WIRE (for WIP-related) [21].
  • Third, a fusion protein of WIP to WASP efficiently mediates NFAT activation [22].

Analytical, diagnostic and therapeutic context of WIPF1

  • Immunofluorescence localization of WIP in yeast cells reveals a pattern consistent with its function at the cortical sites of growth [8].
  • The Microsphere Units from BRACE can be customer tailored to the materials and all necessary specifications as FDA, GMP/GLP, EX, CIP, WIP etc [23].
  • Since 1985, the EEG has operated a network of air monitoring sites around WIPP and in nearby communities [24].


  1. Grb2 and Nck act cooperatively to promote actin-based motility of vaccinia virus. Scaplehorn, N., Holmström, A., Moreau, V., Frischknecht, F., Reckmann, I., Way, M. Curr. Biol. (2002) [Pubmed]
  2. The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs. Zettl, M., Way, M. Curr. Biol. (2002) [Pubmed]
  3. Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome. Volkman, B.F., Prehoda, K.E., Scott, J.A., Peterson, F.C., Lim, W.A. Cell (2002) [Pubmed]
  4. National guidelines for infection control in The Netherlands. van den Broek, P.J. J. Hosp. Infect. (1999) [Pubmed]
  5. Conditional uncertainty analysis and implications for decision making: the case of WIPP. Paté-Cornell, M.E. Risk Anal. (1999) [Pubmed]
  6. WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation. Antón, I.M., de la Fuente, M.A., Sims, T.N., Freeman, S., Ramesh, N., Hartwig, J.H., Dustin, M.L., Geha, R.S. Immunity (2002) [Pubmed]
  7. Waltzing with WASP. Ramesh, N., Antón, I.M., Martínez-Quiles, N., Geha, R.S. Trends Cell Biol. (1999) [Pubmed]
  8. The human WASP-interacting protein, WIP, activates the cell polarity pathway in yeast. Vaduva, G., Martinez-Quiles, N., Anton, I.M., Martin, N.C., Geha, R.S., Hopper, A.K., Ramesh, N. J. Biol. Chem. (1999) [Pubmed]
  9. Cortactin interacts with WIP in regulating Arp2/3 activation and membrane protrusion. Kinley, A.W., Weed, S.A., Weaver, A.M., Karginov, A.V., Bissonette, E., Cooper, J.A., Parsons, J.T. Curr. Biol. (2003) [Pubmed]
  10. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Sasahara, Y., Rachid, R., Byrne, M.J., de la Fuente, M.A., Abraham, R.T., Ramesh, N., Geha, R.S. Mol. Cell (2002) [Pubmed]
  11. A complex of Wiskott-Aldrich syndrome protein with mammalian verprolins plays an important role in monocyte chemotaxis. Tsuboi, S. J. Immunol. (2006) [Pubmed]
  12. WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Ramesh, N., Antón, I.M., Hartwig, J.H., Geha, R.S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  13. The expression of Wiskott-Aldrich syndrome protein (WASP) is dependent on WASP-interacting protein (WIP). Konno, A., Kirby, M., Anderson, S.A., Schwartzberg, P.L., Candotti, F. Int. Immunol. (2007) [Pubmed]
  14. Formation of a WIP-, WASp-, actin-, and myosin IIA-containing multiprotein complex in activated NK cells and its alteration by KIR inhibitory signaling. Krzewski, K., Chen, X., Orange, J.S., Strominger, J.L. J. Cell Biol. (2006) [Pubmed]
  15. WIP is a chaperone for Wiskott-Aldrich syndrome protein (WASP). de la Fuente, M.A., Sasahara, Y., Calamito, M., Antón, I.M., Elkhal, A., Gallego, M.D., Suresh, K., Siminovitch, K., Ochs, H.D., Anderson, K.C., Rosen, F.S., Geha, R.S., Ramesh, N. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  16. WIP Regulates the Stability and Localization of WASP to Podosomes in Migrating Dendritic Cells. Chou, H.C., Ant??n, I.M., Holt, M.R., Curcio, C., Lanzardo, S., Worth, A., Burns, S., Thrasher, A.J., Jones, G.E., Calle, Y. Curr. Biol. (2006) [Pubmed]
  17. WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1alpha. Gallego, M.D., de la Fuente, M.A., Anton, I.M., Snapper, S., Fuhlbrigge, R., Geha, R.S. Int. Immunol. (2006) [Pubmed]
  18. The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck. Antón, I.M., Lu, W., Mayer, B.J., Ramesh, N., Geha, R.S. J. Biol. Chem. (1998) [Pubmed]
  19. Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein. Stewart, D.M., Tian, L., Nelson, D.L. J. Immunol. (1999) [Pubmed]
  20. Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1. Scott, M.P., Zappacosta, F., Kim, E.Y., Annan, R.S., Miller, W.T. J. Biol. Chem. (2002) [Pubmed]
  21. The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor receptor. Aspenström, P. Exp. Cell Res. (2002) [Pubmed]
  22. Structure-function analysis of the WIP role in T cell receptor-stimulated NFAT activation: evidence that WIP-WASP dissociation is not required and that the WIP NH2 terminus is inhibitory. Dong, X., Patino-Lopez, G., Candotti, F., Shaw, S. J. Biol. Chem. (2007) [Pubmed]
  23. Preparation of monodisperse controlled release microcapsules. Brandau, T. International journal of pharmaceutics. (2002) [Pubmed]
  24. Issues in establishing an aerosol radiological baseline for the waste isolation pilot plant near Carlsbad, New Mexico. Rodgers, J.C., Kenney, J.W. Health physics. (1997) [Pubmed]
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