The major SHP-1-binding, tyrosine-phosphorylated protein in macrophages is a member of the KIR/LIR family and an SHP-1 substrate

Karen L. Berg, Kristen Carlberg, Larry R. Rohrschneider, Katherine A. Siminovitch, E. Richard Stanley

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

The SH2 domain-containing cytoplasmic protein tyrosine phosphatase, SHP-1, negatively regulates hematopoietic cell signaling. SHP-1 is associated with a tyrosine phosphorylated, plasma membrane-spanning glycoprotein, pp130, in colony stimulating factor-1 stimulated or unstimulated macrophages. This association is phosphotyrosine dependent and is mediated by the amino-terminal SH2 domain of SHP-1. pp130 behaves as a substrate of SHP-1 in vitro and is hyperphosphorylated on tyrosine in SHP-1 deficient macrophages from viable-motheaten mice. Co-immunoprecipitation data indicate that pp130 is the product of the mouse p91/PIR-B gene that encodes a member of the killer cell inhibitory receptor (KIR)/leukocyte immunoglobulin-like receptor (LIR) family. By analogy to the KIRs, p91/PIR-B may represent a novel class of macrophage receptors which act to suppress macrophage activation. These observations identify SHP-1 interactions with and regulation of p91/PIR-B as a potential mechanism for inhibiting the signaling cascades linking extracellular stimuli to macrophage activation and/or development.

Original languageEnglish (US)
Pages (from-to)2535-2541
Number of pages7
JournalOncogene
Volume17
Issue number19
DOIs
StatePublished - Nov 12 1998

Keywords

  • KIR
  • LIR-1
  • Macrophage
  • PIR-B
  • PTP
  • SHP-1

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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