The N-terminal domains of tensin and auxilin are phosphatase homologues

D T Haynie, C P Ponting

Research output: Contribution to journalArticlepeer-review

Abstract

Tensin, an actin filament capping protein, and auxilin, a component of receptor-mediated endocytosis, are known to have 350 residue regions of significant sequence similarity near their N-termini (Schröder et al., 1995, Eur J Biochem 228:297-304). Here we demonstrate that these regions are homologous, not only to each other, but also to the catalytic domain of a putative protein tyrosine phosphatase (PTP) from Saccharomyces cerevisiae and to other PTPs. We propose that the PTP-like portion of the homology region of tensin and auxilin represents a distinct domain. A detailed sequence comparison indicates that the PTP-like domain in tensin is unlikely to exhibit phosphatase activity, whereas in auxilin it may possess a different phosphatase specificity from tyrosine phosphatases. It is probable that the PTP-like domains in tensin and auxilin mediate binding interactions with phosphorylated polypeptides; they may therefore represent members of a distinct class of phosphopeptide recognition domain.

Original languageEnglish
Pages (from-to)2643-6
Number of pages4
JournalProtein Science
Volume5
Issue number12
DOIs
Publication statusPublished - Dec 1996

Keywords

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chickens
  • Microfilament Proteins
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Phosphoric Monoester Hydrolases
  • Sequence Alignment
  • Sequence Analysis
  • Sequence Homology, Amino Acid

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