Ontology highlight
ABSTRACT:
SUBMITTER: Ungureanu D
PROVIDER: S-EPMC4504201 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Nature structural & molecular biology 20110814 9
Human JAK2 tyrosine kinase mediates signaling through numerous cytokine receptors. The JAK2 JH2 domain functions as a negative regulator and is presumed to be a catalytically inactive pseudokinase, but the mechanism(s) for its inhibition of JAK2 remains unknown. Mutations in JH2 lead to increased JAK2 activity, contributing to myeloproliferative neoplasms (MPNs). Here we show that JH2 is a dual-specificity protein kinase that phosphorylates two negative regulatory sites in JAK2: Ser523 and Tyr57 ...[more]