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• W1971831341 startingPage "1041" @default.
• W1971831341 abstract "Plastins (fimbrins) are a family of three tissue-specific actin-binding proteins. Both L- and T-plastin have been shown to be involved in cytoskeletal reorganization in signal-transduction pathways. Phosphorylation of the leukocyte-specific L-plastin plays important roles in regulating L-plastin function and leukocyte activation. We created L-plastin mutants, changing each of the Ser-5 and Ser-7 residues to alanine. Expression of either mutant in WI38VA13 fibroblasts did not result in phosphorylation. The transfected wildtype L-plastin was phosphorylated in WI38VA13, but its two-dimensional gel pattern suggested that it was phosphorylated on one residue, whereas the endogenous L-plastin in leukocytes was likely phosphorylated on two residues. The nonleukocyte-specific T-plastin, which has an equivalent Ser-7 residue, was not phosphorylated in T-plastinexpressing fibroblasts or in transfected leukocytes. Expression of CK-IIα, the catalytic subunit of casein kinase II, resulted in changes of the protein expression profile in leukocytes but not the phosphorylation status of L- or T-plastin. Phorbol myristate acetate induced L-plastin phosphorylation in both leukocytes and fibroblasts, lending support to the view that protein kinase C is the likely candidate kinase for L-plastin phosphorylation." @default.
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• W1971831341 creator A5087300539 @default.
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• W1971831341 date "1998-12-01" @default.
• W1971831341 modified "2023-09-25" @default.
• W1971831341 title "Analysis and Mapping of Plastin Phosphorylation" @default.
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• W1971831341 doi "https://doi.org/10.1089/dna.1998.17.1041" @default.
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