rdf:type |
|
lifeskim:mentions |
umls-concept:C0010531,
umls-concept:C0018042,
umls-concept:C0020792,
umls-concept:C0025255,
umls-concept:C0067533,
umls-concept:C0086418,
umls-concept:C0220905,
umls-concept:C0229613,
umls-concept:C0242210,
umls-concept:C0330390,
umls-concept:C1510827,
umls-concept:C1711351
|
pubmed:issue |
5
|
pubmed:dateCreated |
1992-6-16
|
pubmed:abstractText |
Immunocytochemical evidence of an association between the regulatory subunit RII of the cAMP-dependent protein kinase (cAMP-PK) and the Golgi apparatus in several cell types has been reported. In order to identify endogenous Golgi proteins binding RII, a fraction enriched in Golgi vesicles was isolated from human lymphoblasts. Only the RII beta isoform was detected in the Golgi-rich fraction, although RII alpha has also been found to be present in these cells. A 85 kDa RII-binding protein was identified in Golgi vesicles using a [32P]RII overlay of Western blots. The existence of an endogenous RII beta-p85 complex in isolated Golgi vesicles was demonstrated by two independent means: (i) co-immunoprecipitation of both proteins under non-denaturing conditions with an antibody against RII beta and (ii) co-purification of RII beta-p85 complexes on a cAMP-analogue affinity column. p85 was phosphorylated by both endogenous and purified catalytic subunits of cAMP-pKII. Extraction experiments and protease protection experiments indicated that p85 is an integral membrane protein although it partitioned atypically during Triton X-114 phase separation. We propose that p85 anchors RII beta to the Golgi apparatus of human lymphoblasts and thereby defines the Golgi substrate targets most accessible to phosphorylation by C subunit. This mechanism may be relevant to the regulation of processes involving the Golgi apparatus itself, such as membrane traffic and secretion, but also relevant to nearby nuclear events dependent on C subunit.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1582408-16921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1582408-1826763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1582408-1860836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1582408-1918018,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1582408-942051
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0261-4189
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
11
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1723-31
|
pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1582408-Humans,
pubmed-meshheading:1582408-Animals,
pubmed-meshheading:1582408-Cattle,
pubmed-meshheading:1582408-Lymphocytes,
pubmed-meshheading:1582408-Golgi Apparatus,
pubmed-meshheading:1582408-Phosphorylation,
pubmed-meshheading:1582408-Microscopy, Fluorescence,
pubmed-meshheading:1582408-Autoradiography,
pubmed-meshheading:1582408-Membrane Proteins,
pubmed-meshheading:1582408-Precipitin Tests
|