[HTML][HTML] Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization: association of JAK2 with the GHR is enhanced by receptor …
Y Zhang, J Jiang, JJ Kopchick, SJ Frank - Journal of Biological Chemistry, 1999 - ASBMB
The growth hormone (GH) receptor (GHR) binds GH in its extracellular domain and
transduces activating signals via its cytoplasmic domain. Both GH-induced GHR
dimerization and JAK2 tyrosine kinase activation are critical in initiation of GH signaling. We
previously described a rapid GH-induced disulfide linkage of GHRs in human IM-9 cells. In
this study, three GH-induced phenomena (GHR dimerization, GHR disulfide linkage, and
enhanced GHR-JAK2 association) were examined biochemically and immunologically. By …
transduces activating signals via its cytoplasmic domain. Both GH-induced GHR
dimerization and JAK2 tyrosine kinase activation are critical in initiation of GH signaling. We
previously described a rapid GH-induced disulfide linkage of GHRs in human IM-9 cells. In
this study, three GH-induced phenomena (GHR dimerization, GHR disulfide linkage, and
enhanced GHR-JAK2 association) were examined biochemically and immunologically. By …
