C-terminal binding: An expanded repertoire and function of 14-3-3 proteins

Brian Coblitz, Meng Wu, Sojin Shikano, Min Li

Research output: Contribution to journalShort survey

Abstract

Amino and carboxyl termini are unique positions in a polypeptide. They tend to be exposed in folded three dimensional structures. Diversity and functional significance of C-terminal sequences have been appreciated from studies of PDZ and PEX domains. Signaling 14-3-3 protein signaling by recognizing phosphorylated peptides plays a critical role in a variety of biological processes, including oncogenesis. The preferential binding of 14-3-3 to phosphorylated C-terminal sequences, mode III, provides a means of regulated binding and considerably expands the substrate repertoire of 14-3-3 interaction partners.

Original languageEnglish (US)
Pages (from-to)1531-1535
Number of pages5
JournalFEBS Letters
Volume580
Issue number6
DOIs
StatePublished - Mar 6 2006

Keywords

  • 14-3-3
  • Binding assay
  • Binding motif
  • C-terminal
  • Cancer signaling
  • Fluorescence anisotropy
  • Mode III
  • Phosphorylation
  • SWTY

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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