Wip: More than a wasp-interacting protein

Sophia Fried, Omri Matalon, Elad Noy, Mira Barda-Saad*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


WIP plays an important role in the remodeling of the actin cytoskeleton, which controls cellular activation, proliferation, and function. WIP regulates actin polymerization by linking the actin machinery to signaling cascades. WIP binding to WASp and to its homolog, N-WASp, which are central activators of the actin-nucleating complex Arp2/3, regulates their cellular distribution, function, and stability. By binding to WASp, WIP protects it from degradation and thus, is crucial for WASp retention. Indeed, most mutations that result in WAS, an X-linked immunodeficiency caused by defective/absent WASp activity, are located in the WIP-binding region of WASp. In addition, by binding directly to actin, WIP promotes the formation and stabilization of actin filaments. WASp-independent activities of WIP constitute a new research frontier and are discussed extensively in this article. Here, we review the current information on WIP in human and mouse systems, focusing on its associated proteins, its molecular-regulatory mechanisms, and its role as a key regulator of actinbased processes in the immune system.

Original languageEnglish
Pages (from-to)723-727
Number of pages5
JournalJournal of Leukocyte Biology
Issue number5
StatePublished - 1 Nov 2014
Externally publishedYes


  • Actin polymerization
  • Cytoskeleton
  • Immune cells
  • Immune synapse
  • Lymphocytes


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