Homodimerization and intermolecular tyrosine phosphorylation of the Tyk-2 tyrosine kinase.
The Jak kinases and Stat transcription factors play a major role in signaling of various cytokines including IFN alpha. In this report we show a ligand-independent interaction between Tyk-2 and Jak-1 kinases. We also demonstrate that the Tyk-2 kinase forms a homodimer that has the ability to undergo intermolecular tyrosine phosphorylation. The formation of the Tyk-2 homodimer is independent of both tyrosine phosphorylation and the presence of the tyrosine kinase domain.
Domanski
P
P
Department of Pathology, University of Tennessee, Memphis 88163, USA.
Yan
H
H
Witte
M M
MM
Krolewski
J
J
Colamonici
O R
OR
D002460:Cell Line; D015870:Gene Expression; D006367:HeLa Cells; D006801:Humans; D015151:Immunoblotting; D007370:Interferon Type I / Q000494:pharmacology; D053613:Janus Kinase 1; D046911:Macromolecular Substances; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000235:genetics / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins; D015398:Signal Transduction; D053634:TYK2 Kinase; D014162:Transfection
D007370:Interferon Type I; D046911:Macromolecular Substances; D011506:Proteins; D011994:Recombinant Proteins; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases; C507904:JAK1 protein, human; D053613:Janus Kinase 1; D053634:TYK2 Kinase; C070139:TYK2 protein, human