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Generation and characterization of a novel, permanently active S100P mutant

Generation and characterization of a novel, permanently active S100P mutant

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AUSTERMANN, Judith, Ali Reza NAZMI, Annika HEIL, Günter FRITZ, Michal KOLINSKI, Slawomir FILIPEK, Volker GERKE, 2009. Generation and characterization of a novel, permanently active S100P mutant. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier. 1793(6), pp. 1078-1085. ISSN 0167-4889. eISSN 1879-2596. Available under: doi: 10.1016/j.bbamcr.2008.11.012

@article{Austermann2009-06Gener-58103, title={Generation and characterization of a novel, permanently active S100P mutant}, year={2009}, doi={10.1016/j.bbamcr.2008.11.012}, number={6}, volume={1793}, issn={0167-4889}, journal={Biochimica et Biophysica Acta (BBA) - Molecular Cell Research}, pages={1078--1085}, author={Austermann, Judith and Nazmi, Ali Reza and Heil, Annika and Fritz, Günter and Kolinski, Michal and Filipek, Slawomir and Gerke, Volker} }

Fritz, Günter Kolinski, Michal Filipek, Slawomir Nazmi, Ali Reza 2022-07-21T06:40:38Z Gerke, Volker Austermann, Judith Filipek, Slawomir Heil, Annika 2009-06 Kolinski, Michal Heil, Annika Gerke, Volker Fritz, Günter S100 proteins function as Ca<sup>2+</sup> signal transducers by regulating cellular targets in their Ca<sup>2+</sup> bound conformation. S100P is a member of the S100 protein family that can activate the membrane and F-actin binding protein ezrin in a Ca<sup>2+</sup> dependent manner at least in vitro. Here we generated a novel tool to elucidate directly the S100P–ezrin interaction in vivo. This was achieved by constructing a S100P derivative that contained mutations in the two EF hand loops predicted to lock the protein in a permanently active state. The resulting S100P mutant, termed here S100P pa, could be purified as a soluble protein and showed biochemical properties displayed by wild-type S100P only in the presence of Ca<sup>2+</sup>. Importantly, S100P pa bound to the N-terminal domain of ezrin in the absence of Ca<sup>2+</sup> showing an affinity only slightly reduced as compared to that of Ca<sup>2+</sup>-bound WT S100P. In line with this permanent complex formation, S100P pa colocalized with ezrin to plasma membrane protrusions of epithelial cells even in the absence of intracellular Ca<sup>2+</sup> transients. Thus, S100P pa is a novel type of S100 protein mutant locked in a permanently active state that shows an unregulated complex formation with its cellular target ezrin. eng Generation and characterization of a novel, permanently active S100P mutant 2022-07-21T06:40:38Z Austermann, Judith Nazmi, Ali Reza

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