RGD Reference Report - The zinc- and calcium-binding S100B interacts and co-localizes with IQGAP1 during dynamic rearrangement of cell membranes. - Rat Genome Database

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The zinc- and calcium-binding S100B interacts and co-localizes with IQGAP1 during dynamic rearrangement of cell membranes.

Authors: Mbele, GO  Deloulme, JC  Gentil, BJ  Delphin, C  Ferro, M  Garin, J  Takahashi, M  Baudier, J 
Citation: Mbele GO, etal., J Biol Chem 2002 Dec 20;277(51):49998-50007.
RGD ID: 727451
Pubmed: PMID:12377780   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M205363200   (Journal Full-text)

The Zn(2+)- and Ca(2+)-binding S100B protein is implicated in multiple intracellular and extracellular regulatory events. In glial cells, a relationship exists between cytoplasmic S100B accumulation and cell morphological changes. We have identified the IQGAP1 protein as the major cytoplasmic S100B target protein in different rat and human glial cell lines in the presence of Zn(2+) and Ca(2+). Zn(2+) binding to S100B is sufficient to promote interaction with IQGAP1. IQ motifs on IQGAP1 represent the minimal interaction sites for S100B. We also provide evidence that, in human astrocytoma cell lines, S100B co-localizes with IQGAP1 at the polarized leading edge and areas of membrane ruffling and that both proteins relocate in a Ca(2+)-dependent manner within newly formed vesicle-like structures. Our data identify IQGAP1 as a potential target protein of S100B during processes of dynamic rearrangement of cell membrane morphology. They also reveal an additional cellular function for IQGAP1 associated with Zn(2+)/Ca(2+)-dependent relocation of S100B.

Objects referenced in this article
Gene S100b S100 calcium binding protein B Rattus norvegicus

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