Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1987-2-6
pubmed:abstractText
The GDP-bound alpha subunit of transducin, but not the guanosine 5'-[gamma-thio]triphosphate-bound one, undergoes phosphorylation on tyrosine residues by the insulin receptor kinase and on serine residues by protein kinase C. Holotransducin is poorly phosphorylated by the insulin receptor kinase and is not phosphorylated by protein kinase C. Neither holotransducin nor any of its subunits were phosphorylated by the cAMP-dependent protein kinase. That a given subunit of transducin undergoes multisite phosphorylation depending on the type of nucleotide bound to it or the nature of the kinase suggests that hormone-dependent phosphorylation could provide a versatile mode for regulation of guanine nucleotide-binding protein (G protein) function. In particular, the findings that certain G proteins serve as substrates for both the insulin receptor kinase and protein kinase C implicate G proteins in playing a key role in mediating the action of insulin and ligands that act to activate protein kinase C.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-188466, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-212737, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-2856889, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3001088, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3079907, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3158511, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3161729, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3896232, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3897231, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3919382, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3920212, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3922971, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-3923487, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-5162297, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6093803, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6101903, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6136510, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6142883, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6150041, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6236809, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6240439, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6246487, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6269165, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6288684, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6294652, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6300694, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6304074, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6305976, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6316958, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6336757, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6339486, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6417656, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6704089, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6757253, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-6766444, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-7031900, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-7085651, http://linkedlifedata.com/resource/pubmed/commentcorrection/3099281-7276563
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9294-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Multisite phosphorylation of the alpha subunit of transducin by the insulin receptor kinase and protein kinase C.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't