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We provide comprehensive proteomic and phosphoproteomic analyses to identify phosphorylation/dephosphorylation substrates of the highly conserved striatin-interacting phosphatases and kinases (STRIPAK) complex. Among the putative targets of STRIPAK, we identified CLA4, a member of the p21-activated kinase (PAK) family. Functional analysis of both phospho-mimetic and -deficient protein variants demonstrate that STRIPAK regulates phosphorylation of CLA4.

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This page is a summary of: Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth, Molecular Microbiology, February 2020, Wiley,
DOI: 10.1111/mmi.14475.
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