Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis

Guo Zhong Tao, Celeste Kirby, Stephen A. Whelan, Frank Rossi, Xiahui Bi, Michael MacLaren, Erik Gentalen, Roger A. O'Neill, Gerald Warren Hart, M. Bishr Omary

Research output: Contribution to journalArticle

Abstract

Phosphorylation and O-GlcNAcylation of keratin 18 (K18) are highly dynamic and involve primarily independent K18 populations. We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other. The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation. Our findings support the reciprocity of these two post-translational modifications. Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.

Original languageEnglish (US)
Pages (from-to)708-712
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume351
Issue number3
DOIs
StatePublished - Dec 22 2006

Keywords

  • Intermediate filaments
  • Keratin 18
  • O-GlcNAc transferase
  • O-GlcNAcylation
  • O-Glycosylation
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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  • Cite this

    Tao, G. Z., Kirby, C., Whelan, S. A., Rossi, F., Bi, X., MacLaren, M., Gentalen, E., O'Neill, R. A., Hart, G. W., & Omary, M. B. (2006). Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis. Biochemical and Biophysical Research Communications, 351(3), 708-712. https://doi.org/10.1016/j.bbrc.2006.10.092