Prlr associates with Jak2

Stable Identifier
Reaction [binding]
Rattus norvegicus
SVG |   | PPTX  | SBGN
Prlr associates with Jak2
Prlr has no intrinsic kinase activity but associates with Janus kinase 2 (Jak2) (Lebrun et al. 1994, 1995) which is bound and activated following receptor activation (Campbell et al. 1994, Rui et al. 1994, Carter-Su et al. 2000, Barua et al. 2009). The box 1 region of Prlr, a membrane proximal proline-rich region in the intracellular domain conserved in all members of the growth hormone rereptor family, is critical for Jak2 association. Deletion of this region virtually abolishes Prlr signaling (Edery et al. 1994). Alanine substitutions of individual residues within box 1 of rat Prlr have shown that the most C-terminal proline (P250) is critical for association with and subsequent activation of Jak2 (Pezet et al. 1997). When the receptor is activated by ligand binding, it binds Jak2. Jak2 itself becomes activated and phosphorylates the dimerized receptor. This is followed by phosphorylation, dimerization and nuclear translocation of Stat5. There are nine other tyrosines in the cytoplasmic domain, some of which may undergo phosphorylation and may participate in signal transduction.
Literature References
PubMed ID Title Journal Year
7537736 Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction

Lebrun, JJ, Kelly, PA, Ullrich, A, Ali, S

J Biol Chem 1995
7515493 Activation of JAK2 tyrosine kinase by prolactin receptors in Nb2 cells and mouse mammary gland explants

Carter-Su, C, Campbell, GS, Argetsinger, LS, Kelly, PA, Rillema, JA, Ihle, JN

Proc Natl Acad Sci U S A 1994
7508935 Activation of receptor-associated tyrosine kinase JAK2 by prolactin

Farrar, WL, Rui, H, Kirken, RA

J Biol Chem 1994
8188682 Prolactin-induced proliferation of Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2

Lebrun, JJ, Kelly, PA, Ullrich, A, Sofer, L, Ali, S

J Biol Chem 1994
Orthologous Events
Cite Us!