Regulation of Wiskott-Aldrich syndrome protein and related molecules.

Caron E

doi:10.1016/s0955-0674(01)00298-8

Regulation of Wiskott-Aldrich syndrome protein and related molecules.

Caron E ¹

Affiliations

1. MRC-LMCB and Cell Biology Unit, University College London, Gower Street, WC1E 6BT, London, UK.
Authors
Caron E¹
(1 author)

Current Opinion in Cell Biology, 01 Feb 2002, 14(1):82-87
https://doi.org/10.1016/s0955-0674(01)00298-8 PMID: 11792549

Review

Abstract

Wiskott-Aldrich syndrome protein (WASP), the gene mutated in the haematological disorder Wiskott-Aldrich syndrome, is the founding member of a family of conserved cytoskeletal regulators. WASP family proteins regulate actin dynamics through binding and activation of the Arp2/3 complex, which nucleates new actin filaments. Recently, a huge amount of information on WASPs has become available, both in terms of the function of individual domains, identification of their binding partners, and the unravelling of complex regulatory mechanisms. Together, these new findings place WASP-related molecules at the crossroads between distinct signalling pathways, which they integrate into coherent cytoskeletal responses.

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References

Articles referenced by this article (55)

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Clinical Features and Outcomes of 23 Patients with Wiskott-Aldrich Syndrome: A Single-Center Experience
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This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
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Close encounters of the third kind: disordered domains and the interactions of proteins.
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WASP and WIP regulate podosomes in migrating leukocytes.
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Free full text in Europe PMC
The WAVE2/Abi1 complex differentially regulates megakaryocyte development and spreading: implications for platelet biogenesis and spreading machinery.
Eto K, Nishikii H, Ogaeri T, Suetsugu S, Kamiya A, Kobayashi T, Yamazaki D, Oda A, Takenawa T, Nakauchi H
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Cited by: 32 articles | PMID: 17664349

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Regulation of Wiskott-Aldrich syndrome protein and related molecules.

Affiliations

Authors

Abstract

Full text links

References

The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization.

Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex.

Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex.

Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins.

Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex.

Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP.

Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization.

Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP.

Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3.

Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.

Citations & impact

Impact metrics

Citations of article over time

Smart citations by scite.ai
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1016/s0955-0674(01)00298-8

Article citations

Clinical Features and Outcomes of 23 Patients with Wiskott-Aldrich Syndrome: A Single-Center Experience

Close encounters of the third kind: disordered domains and the interactions of proteins.

WASP and WIP regulate podosomes in migrating leukocytes.

Specialized podosome- or invadopodia-like structures (PILS) for focal trabecular meshwork extracellular matrix turnover.

The WAVE2/Abi1 complex differentially regulates megakaryocyte development and spreading: implications for platelet biogenesis and spreading machinery.

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Regulation of Wiskott-Aldrich syndrome protein and related molecules.

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