Extracellular signals and reversible protein phosphorylation: what to Mek of it all
CM Crews, RL Erikson - Cell, 1993 - cell.com
CM Crews, RL Erikson
Cell, 1993•cell.comErythropoietin (EPO) regulates the proliferation and differentiation of erythroid cells through
interaction with its receptor (EPOR). Although EPOR is a member of the cytokine receptor
superfamily and lacks a kinase domain, EPO induces tyrosine phosphorylation, which is
correlated with gene transcription and mitogenesis. Here we demonstrate that EPO induces
tyrosine phosphorylation of JAK2 kinase and activates its in vitro autophosphorylation. Using
EPOR mutants, phosphorylation and activation of kinase activity correlate with the induction …
interaction with its receptor (EPOR). Although EPOR is a member of the cytokine receptor
superfamily and lacks a kinase domain, EPO induces tyrosine phosphorylation, which is
correlated with gene transcription and mitogenesis. Here we demonstrate that EPO induces
tyrosine phosphorylation of JAK2 kinase and activates its in vitro autophosphorylation. Using
EPOR mutants, phosphorylation and activation of kinase activity correlate with the induction …
Erythropoietin (EPO) regulates the proliferation and differentiation of erythroid cells through interaction with its receptor (EPOR). Although EPOR is a member of the cytokine receptor superfamily and lacks a kinase domain, EPO induces tyrosine phosphorylation, which is correlated with gene transcription and mitogenesis. Here we demonstrate that EPO induces tyrosine phosphorylation of JAK2 kinase and activates its in vitro autophosphorylation. Using EPOR mutants, phosphorylation and activation of kinase activity correlate with the induction of mitogenesis.
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