Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1763, Issue 11, Pages 1284-1297Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2006.08.024
Keywords
S100B; calcium-binding protein; S100 protein; p53; Hdm2; Mdm2
Categories
Funding
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [R01 CA107331, CA 107331] Funding Source: Medline
- NCRR NIH HHS [S10 RR 15741, S10 RR 16812, S10 RR 10441, S10 RR029601] Funding Source: Medline
- NIGMS NIH HHS [R01 GM058888, GM 58888] Funding Source: Medline
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S100B is an EF-hand containing calcium-binding protein of the S100 protein family that exerts its biological effect by binding and affecting various target proteins. A consensus sequence for S100B target proteins was published as (K/R)(L/I)xWxxIL and matches a region in the actin capping protein CapZ (VV. Ivanenkov, G.A. Jamieson, Jr., E. Gruenstein, R.V. Dimlich, Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ, J. Biol. Chem. 270 (1995) 14651-14658). Several additional S100B targets are known including p53, a nuclear Dbf2 related (NDR) kinase, the RAGE receptor, neuromodulin, protein kinase C, and others. Examining the binding sites of such targets and new protein sequence searches provided additional potential target proteins for S100B including Hdm2 and Hdm4, which were both found to bind S100B in a calcium-dependent manner. The interaction between S100B and the Hdm2 and/or the Hdm4 proteins may be important physiologically in light of evidence that like Hdm2, S100B also contributes to lowering protein levels of the tumor suppressor protein, p53. For the S100B-p53 interaction, it was found that phosphorylation of specific serine and/or threonine residues reduces the affinity of the S10B-p53 interaction by as much as an order of magnitude, and is important for protecting p53 from S100B-dependent downregulation, a scenario that is similar to what is found for the Hdm2-p53 complex. (c) 2006 Elsevier B.V. All rights reserved.
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