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Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1
Author(s) -
Barišić Sandra,
Nagel Anja C,
FranzWachtel Mirita,
Macek Boris,
Preiss Anette,
Link Gisela,
Maier Dieter,
Hausser Angelika
Publication year - 2011
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2011.53
Subject(s) - phosphorylation , phosphatase , cofilin , microbiology and biotechnology , biochemistry , protein phosphorylation , kinase , chemistry , biology , protein kinase a , cytoskeleton , cell , actin cytoskeleton
By using mass spectrometry, we have identified Ser 402 as a new phosphorylation site within the catalytic domain of human slingshot 1 (SSH1). Phosphorylation at this site inhibits substrate binding and, thus, phosphatase activity in vitro , resulting in enrichment of phosphorylated cofilin in monolayer cell culture. We further demonstrate that protein kinase D (PKD) is upstream from Ser 402 phosphorylation. Accordingly, expression of active PKD in Drosophila phenotypically mimics the loss of SSH activity by inducing accumulation of phosphorylated cofilin and filamentous actin. We thus identify a universal mechanism by which PKD controls SSH1 phosphatase activity.