FRS2 Family Docking Proteins With Overlapping Roles in Activation of MAP Kinase Have Distinct Spatial-Temporal Patterns of Expression of Their Transcripts

FEBS Lett. 2004 Apr 23;564(1-2):14-8. doi: 10.1016/S0014-5793(04)00287-X.

Abstract

FRS2alpha and FRS2beta, two members of the FRS2 family of docking proteins, become tyrosine phosphorylated in response to fibroblast growth factor (FGF) or nerve growth factor (NGF) stimulation. Tyrosine phosphorylated FRS2alpha serves as a platform for the recruitment of multiple signaling proteins for activation of the Ras-mitogen-activated protein (MAP) kinase signaling cascade. We report that Frs2alpha and Frs2beta have distinct spatio-temporal expression patterns in mouse embryos. We further show that FRS2beta can compensate for the loss of FRS2alpha for activation of MAP kinase when expressed in fibroblasts from Frs2alpha(-/-) mouse embryos. We propose that the FRS2 family proteins have distinct roles in vivo through activation of common signaling proteins including MAP kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology*
  • Embryo, Mammalian
  • Fibroblasts / metabolism
  • Gene Expression Regulation, Developmental
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Lipoproteins / genetics
  • Lipoproteins / metabolism
  • Lipoproteins / physiology*
  • Mice
  • Mice, Knockout
  • Mitogen-Activated Protein Kinases / metabolism*
  • Protein Binding
  • RNA, Messenger / analysis
  • RNA, Messenger / biosynthesis*
  • Signal Transduction
  • Time Factors
  • Tissue Distribution

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • FRS3 protein, human
  • Frs3 protein, mouse
  • Intracellular Signaling Peptides and Proteins
  • Lipoproteins
  • RNA, Messenger
  • Mitogen-Activated Protein Kinases