Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction

J Biol Chem. 1994 Aug 12;269(32):20225-8.

Abstract

The role of the protooncogene product p95vav in signal transduction was investigated by characterizing its interactions with proteins that may represent components of a novel signaling pathway. We demonstrate here stable association of p95vav with the heterogeneous ribonucleoprotein K (hnRNP-K), a protein that not only was found to be part of hnRNP particles but has also been implicated in transcriptional regulation of the c-myc gene. Through the PLPPPPPPRG sequence, hnRNP-K specifically interacts with the SH3 domain of p95vav and thus represents a novel SH3 binding protein that may be capable of translating cell surface receptor signals through p95vav activation into regulatory events on the level of gene expression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cell Cycle Proteins*
  • Cell Line
  • Heterogeneous-Nuclear Ribonucleoprotein K
  • Humans
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-vav
  • Ribonucleoproteins / metabolism*
  • Signal Transduction*

Substances

  • Cell Cycle Proteins
  • Heterogeneous-Nuclear Ribonucleoprotein K
  • Oligodeoxyribonucleotides
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-vav
  • Ribonucleoproteins
  • VAV1 protein, human
  • HNRNPK protein, human