Autophosphorylation-dependent protein kinase phosphorylates Ser25, Ser38, Ser65, Ser71, and Ser411 in vimentin and thereby inhibits cytoskeletal intermediate filament assembly

Tze-Jen Huang, Tsong-Tse Lee, Wen-Chuan Lee, Yiu-Kay Lai, Jau-Song Yu, Shiaw-Der Yang

    Research output: Contribution to journalArticlepeer-review

    19 Citations (Scopus)

    Abstract

    The autophosphorylation-dependent protein kinase has been identified as a potent vimentin kinase that incorporates 2 mol of phosphates per mol of protein and generates five major phosphorylation sites in vimentin. Tryptic phosphopeptide mapping by high-performance liquid chromatography followed by sequential manual Edman degradation and direct peptide sequence analysis revealed that Ser-25, Ser-38, Ser-65, and Ser-71 in the amino-terminal domain and Ser-411 in the carboxyl-terminal domain are the phosphorylation sites in vimentin phosphorylated by this kinase, indicating that autophosphorylation-dependent protein kinase is a potent and unique vimentin kinase. Functional study further revealed that phosphorylation of vimentin by autophosphorylation-dependent protein kinase can completely inhibit polymerization and assembly of the cytoskeletal intermediate filament as demonstrated by electron microscopic analysis. Taken together, the results provide initial evidence that the autophosphorylation-dependent protein kinase may function as a vimentin kinase involved in the structure-function regulation of the cytoskeletal system. The results also support the notion that this cyclic nucleotide- and calcium-independent protein kinase may function as a multisubstrate/multifunctional protein kinase involved in the regulation of diverse cell functions.

    Original languageEnglish
    Pages (from-to)517-25
    Number of pages9
    JournalJournal of Protein Chemistry
    Volume13
    Issue number6
    DOIs
    Publication statusPublished - Aug 1994

    Keywords

    • Amino Acid Sequence
    • Animals
    • Intermediate Filaments/chemistry
    • Molecular Sequence Data
    • Phosphorylation
    • Protein Kinases/physiology
    • Serine/metabolism
    • Swine
    • Vimentin/metabolism

    Fingerprint Dive into the research topics of 'Autophosphorylation-dependent protein kinase phosphorylates Ser25, Ser38, Ser65, Ser71, and Ser411 in vimentin and thereby inhibits cytoskeletal intermediate filament assembly'. Together they form a unique fingerprint.

    Cite this