2001
DOI: 10.1016/s1097-2765(01)00401-4
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The N-Terminal Domain of Janus Kinase 2 Is Required for Golgi Processing and Cell Surface Expression of Erythropoietin Receptor

Abstract: We show that Janus kinase 2 (JAK2), and more specifically just its intact N-terminal domain, binds to the erythropoietin receptor (EpoR) in the endoplasmic reticulum and promotes its cell surface expression. This interaction is specific as JAK1 has no effect. Residues 32 to 58 of the JAK2 JH7 domain are required for EpoR surface expression. Alanine scanning mutagenesis of the EpoR membrane proximal region reveals two modes of EpoR-JAK2 interaction. A continuous block of EpoR residues is required for functional… Show more

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Cited by 268 publications
(277 citation statements)
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“…This was demonstrated for JAK2 and Erythropoietin, as well as for JAK1 and Oncostatin M. JAK overexpression was associated with a better transport of the receptor to the cell surface (Huang et al, 2001;Radtke et al, 2002). For the Interferon receptor I, TYK2 was reported to increase cell-surface expression by inhibiting the endocytosis of the receptor (Ragimbeau et al, 2003).…”
Section: Activated Signaling Pathways In Autonomous Clonesmentioning
confidence: 89%
“…This was demonstrated for JAK2 and Erythropoietin, as well as for JAK1 and Oncostatin M. JAK overexpression was associated with a better transport of the receptor to the cell surface (Huang et al, 2001;Radtke et al, 2002). For the Interferon receptor I, TYK2 was reported to increase cell-surface expression by inhibiting the endocytosis of the receptor (Ragimbeau et al, 2003).…”
Section: Activated Signaling Pathways In Autonomous Clonesmentioning
confidence: 89%
“…gp130 is a central determinant of signaling patterns associated with multiple IL-6-type cytokines (51). It directly interacts with principle components of the Jak/STAT pathway, including Jak 1, forming tight and enduring complexes (51)(52)(53). Multiple proline-rich regions of gp130, notably in the box1 region, are critical to Jak 1 binding.…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, this interaction between JAKs and cytokine receptors can regulate receptor localization [101,102]. Specifically, the surface expression of EPO receptors is regulated by the FERM domain of JAK2 [103] and both JAK2 and TYK2 have been shown to inhibit the proteasomal degradation of the thrombopoietin receptor [99]. The selectivity of STAT activation by various ligands is determined mainly by the highly specific interactions between the SH2 domain and the phosphotyrosine residues on each receptor [94].…”
Section: Structure Of Jak Family Proteinsmentioning
confidence: 99%