Growth hormone receptor binds Lyn

Stable Identifier
R-MMU-1168927
Type
Reaction [binding]
Species
Mus musculus
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Growth hormone receptor binds Lyn
There is accumulating evidence that GH signalling utilises a Src family tyrosine kinase independently of JAK2, and that this is linked to activation of extracellular regulated kinases (ERKs) 1 and 2 (p44/42 MAPK). The relative strengths of these signaling pathways probably depends on cell type and may be mediated by conformational changes that are a consequence of ligand binding (Rowlinson et al. 2007). In NIH-3T3 cells GH activated c-Src, which in turn activated ERK1/2 via a pathway involving the activation of the Ras-like small GTPases RalA and RalB, leading to Elk-1 mediated transcription (Zhu et al. 2002). JAK2 and c-Src were both found to activate the Ras-like small GTPases Rap1 and Rap2 which inhibit RalA mediated activation of ERK1/2 (Ling et al. 2003). Src kinase inhibition was found to block ERK activation by GH. The major contributing kinase was identified as Lyn, which was found to co-immunoprecipitate with GHR and bind to the proximal 150 residues of the cytoplasmic domain (Rowlinson et al. 2007).
Literature References
PubMed ID Title Journal Year
18488018 An agonist-induced conformational change in the growth hormone receptor determines the choice of signalling pathway

Rowlinson, SW, Yoshizato, H, Barclay, JL, Brooks, AJ, Behncken, SN, Kerr, LM, Millard, K, Palethorpe, K, Nielsen, K, Clyde-Smith, J, Hancock, JF, Waters, MJ

Nat Cell Biol 2008
Participants
Input
Output
Orthologous Events
Growth hormone receptor binds Lyn (Homo sapiens)
Authored
Jupe, S  (2010-10-14)
Reviewed
Herington, AC  (2011-06-13)
Waters, MJ  (2011-06-23)
Created
Jupe, S  (2011-01-11)
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