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http://purl.uniprot.org/citations/11751854http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11751854http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11751854http://www.w3.org/2000/01/rdf-schema#comment"Activation of JAK tyrosine kinases is an essential step in cell signaling by multiple hormones, cytokines, and growth factors, including growth hormone (GH) and interferon-gamma. Previously, we identified SH2-B beta as a potent activator of JAK2 (Rui, L., and Carter-Su, C. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 7172-7177). Here, we investigated whether the activation of JAK2 by SH2-B beta is specific to JAK2 and SH2-B beta or extends to other JAKs or other members of the SH2-B beta family. When SH2-B beta was overexpressed with JAK1 or JAK3, SH2-B beta failed to increase their activity. However, SH2-B beta bound to both and was tyrosyl-phosphorylated by JAK1. In contrast to SH2-B beta, APS decreased tyrosyl phosphorylation of GH-stimulated JAK2 as well as Stat5B, a substrate of JAK2. APS also decreased tyrosyl phosphorylation of JAK1, but did not affect the activity or tyrosyl phosphorylation of JAK3. Overexpressed APS bound to and was tyrosyl-phosphorylated by all three JAKs. Consistent with these data, in 3T3-F442A adipocytes, endogenous APS was tyrosyl-phosphorylated in response to GH and interferon-gamma. These results suggest that 1) SH2-B beta specifically activates JAK2, 2) APS negatively regulates both JAK2 and JAK1, and 3) both SH2-B beta and APS may serve as adapter proteins for all three JAKs independent of any role they have in JAK activity."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109165200"xsd:string
http://purl.uniprot.org/citations/11751854http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109165200"xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"O'Shea J.J."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"O'Shea J.J."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"Carter-Su C."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"Carter-Su C."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"O'Brien K.B."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/author"O'Brien K.B."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/pages"8673-8681"xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/pages"8673-8681"xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/title"SH2-B family members differentially regulate JAK family tyrosine kinases."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/title"SH2-B family members differentially regulate JAK family tyrosine kinases."xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11751854http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11751854http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11751854
http://purl.uniprot.org/citations/11751854http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11751854
http://purl.uniprot.org/citations/11751854http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11751854
http://purl.uniprot.org/citations/11751854http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11751854