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.
%0 Journal Article
%1 Barisic2011
%A Barisić, Sandra
%A Nagel, Anja C.
%A Franz-Wachtel, Mirita
%A MacEk, Boris
%A Preiss, Anette
%A Link, Gisela
%A Maier, Dieter
%A Hausser, Angelika
%D 2011
%J EMBO Reports
%K 2011 hausser izi
%N 6
%P 527--533
%R 10.1038/embor.2011.53
%T Phosphorylation of ser 402 impedes phosphatase activity of slingshot 1
%U https://www.ncbi.nlm.nih.gov/pubmed/21525957
%V 12
%X 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.
%Z Barisic, SandraNagel, Anja CFranz-Wachtel, MiritaMacek, BorisPreiss, AnetteLink, GiselaMaier, DieterHausser, AngelikaengResearch Support, Non-U.S. Gov'tEnglandEMBO Rep. 2011 Jun;12(6):527-33. doi: 10.1038/embor.2011.53. Epub 2011 Apr 28.
%7 2011/04/29
%@ 1469-3178 (Electronic)$\backslash$r1469-221X (Linking)
@article{Barisic2011,
abstract = {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.},
added-at = {2023-06-29T13:07:55.000+0200},
annote = {Barisic, SandraNagel, Anja CFranz-Wachtel, MiritaMacek, BorisPreiss, AnetteLink, GiselaMaier, DieterHausser, AngelikaengResearch Support, Non-U.S. Gov'tEnglandEMBO Rep. 2011 Jun;12(6):527-33. doi: 10.1038/embor.2011.53. Epub 2011 Apr 28.},
author = {Bari{\v{s}}i{\'{c}}, Sandra and Nagel, Anja C. and Franz-Wachtel, Mirita and MacEk, Boris and Preiss, Anette and Link, Gisela and Maier, Dieter and Hausser, Angelika},
biburl = {https://puma.ub.uni-stuttgart.de/bibtex/28094e00d7baa3373d91c2f9f72aa904b/fabian},
doi = {10.1038/embor.2011.53},
edition = {2011/04/29},
interhash = {452e1e485fd32951a1a7b1be2d45136a},
intrahash = {8094e00d7baa3373d91c2f9f72aa904b},
isbn = {1469-3178 (Electronic)$\backslash$r1469-221X (Linking)},
issn = {1469221X},
journal = {EMBO Reports},
keywords = {2011 hausser izi},
number = 6,
pages = {527--533},
pmid = {21525957},
timestamp = {2023-06-29T13:07:55.000+0200},
title = {{Phosphorylation of ser 402 impedes phosphatase activity of slingshot 1}},
url = {https://www.ncbi.nlm.nih.gov/pubmed/21525957},
volume = 12,
year = 2011
}
