A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival

Biochem Biophys Res Commun. 2000 Apr 2;270(1):267-71. doi: 10.1006/bbrc.2000.2413.

Abstract

To find a possible signal interacting with the Jak3 N-terminal, we screened the human peripheral blood cDNA library through both a two-hybrid system and a tyrosine-phosphorylation-modified two-hybrid system using the N-terminal of Jak3 as bait. Results showed that one new homologue of myosin heavy chain, designated MAJN (molecule associated with Jak3 N-terminal), could bind to Jak3 in a tyrosine-phosphorylation-independent manner. The interaction between Jak3 and MAJN was further confirmed by immunoprecipitation in BAF-B03 beta cells. To investigate the function of MAJN, we have constructed the BAF-B03 beta/MAJN cell line that stably expresses MAJN and found that overexpression of MAJN can partially inhibit the apoptosis induced by interleukin-2 deprival. Further studies are needed to elucidate how MAJN executes its function to antagonize BAF-B03beta cell death in the absence of IL-2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / physiology*
  • Apoptosis Regulatory Proteins
  • Binding Sites
  • Carrier Proteins*
  • Humans
  • Interleukin-2 / deficiency*
  • Janus Kinase 3
  • Mutation
  • Myosin Heavy Chains / genetics
  • Myosin Heavy Chains / metabolism*
  • Nuclear Proteins
  • Precipitin Tests
  • Protein Binding
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Sequence Deletion
  • Two-Hybrid System Techniques

Substances

  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • Interleukin-2
  • Nuclear Proteins
  • TIAF1 protein, human
  • Protein-Tyrosine Kinases
  • JAK3 protein, human
  • Janus Kinase 3
  • Myosin Heavy Chains