A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival.
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.
Mesh Terms:
Apoptosis, Apoptosis Regulatory Proteins, Binding Sites, Carrier Proteins, Humans, Interleukin-2, Janus Kinase 3, Mutation, Myosin Heavy Chains, Nuclear Proteins, Precipitin Tests, Protein Binding, Protein-Tyrosine Kinases, Sequence Deletion, Two-Hybrid System Techniques
Apoptosis, Apoptosis Regulatory Proteins, Binding Sites, Carrier Proteins, Humans, Interleukin-2, Janus Kinase 3, Mutation, Myosin Heavy Chains, Nuclear Proteins, Precipitin Tests, Protein Binding, Protein-Tyrosine Kinases, Sequence Deletion, Two-Hybrid System Techniques
Biochem. Biophys. Res. Commun.
Date: Apr. 02, 2000
PubMed ID: 10733938
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