These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization.
    Author: Miki H, Takenawa T.
    Journal: Biochem Biophys Res Commun; 1998 Feb 04; 243(1):73-8. PubMed ID: 9473482.
    Abstract:
    Verprolin is a yeast protein whose inactivation leads to a cytoskeletal defect characterized by the abnormal organization of actin filaments. Recently, two mammalian proteins previously shown to regulate the actin cytoskeleton, Wiskott-Aldrich Syndrome Protein (WASP) and its homolog expressed in neurons (N-WASP), were found to possess short peptide motifs homologous to one part of verprolin. However, the physiological function of the homologous regions (verprolin-homology domain, VPH domain) remains unknown. Here we report the importance of the VPH domain as the direct actin binding region. In the case of N-WASP, the VPH domain co-acts with the cofilinhomologous region to sever actin filaments in vitro. Furthermore, the VPH domain is indispensable for the reorganization of the actin cytoskeleton by N-WASP downstream of tyrosine kinases in living cells. All data demonstrate that the VPH domain plays critical roles in the regulation of the actin cytoskeleton.
    [Abstract] [Full Text] [Related] [New Search]