Source:http://linkedlifedata.com/resource/pubmed/id/10671526
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2000-3-21
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| pubmed:databankReference | |
| pubmed:abstractText |
cGMP-dependent protein kinase (cGK) is a major cellular receptor of cGMP and plays important roles in cGMP-dependent signal transduction pathways. To isolate the components of the cGMP/cGK signaling pathway such as substrates and regulatory proteins of cGK, we employed the yeast two-hybrid system using cGK-Ialpha as a bait and isolated a novel male germ cell-specific 42-kDa protein, GKAP42 (42-kDa cGMP-dependent protein kinase anchoring protein). Although the N-terminal region (amino acids 1-66) of cGK-Ialpha is sufficient for the association with GKAP42, GKAP42 could not interact with cGK-Ibeta, cGK-II, or cAMP-dependent protein kinase. GKAP42 mRNA is specifically expressed in testis, where it is restricted to the spermatocytes and early round spermatids. Endogenous cGK-I is co-immunoprecipitated with anti-GKAP42 antibody from mouse testis tissue, suggesting that cGK-I physiologically interacts with GKAP42. Immunocytochemical observations revealed that GKAP42 is localized to the Golgi complex and that cGK-Ialpha is co-localized to the Golgi complex when coexpressed with GKAP42. Although both cGK-Ialpha and -Ibeta, but not cAMP-dependent protein kinase, phosphorylated GKAP42 in vitro, GKAP42 was a good substrate only for cGK-Ialpha in intact cells, suggesting that the association with kinase protein is required for the phosphorylation in vivo. Finally, we demonstrated that the kinase-deficient mutant of cGK-Ialpha stably associates with GKAP42 and that binding of cGMP to cGK-Ialpha facilitates their release from GKAP42. These findings suggest that GKAP42 functions as an anchoring protein for cGK-Ialpha and that cGK-Ialpha may participate in germ cell development through phosphorylation of Golgi-associated proteins such as GKAP42.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/cGMP-dependent protein kinase Ialpha
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
18
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| pubmed:volume |
275
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
4897-905
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:10671526-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10671526-Amino Acid Sequence,
pubmed-meshheading:10671526-Animals,
pubmed-meshheading:10671526-Base Sequence,
pubmed-meshheading:10671526-Carrier Proteins,
pubmed-meshheading:10671526-Cattle,
pubmed-meshheading:10671526-Cyclic GMP-Dependent Protein Kinases,
pubmed-meshheading:10671526-DNA, Complementary,
pubmed-meshheading:10671526-Gene Expression Regulation, Developmental,
pubmed-meshheading:10671526-Male,
pubmed-meshheading:10671526-Mice,
pubmed-meshheading:10671526-Molecular Sequence Data,
pubmed-meshheading:10671526-Phosphorylation,
pubmed-meshheading:10671526-Protein Binding,
pubmed-meshheading:10671526-Saccharomyces cerevisiae,
pubmed-meshheading:10671526-Signal Transduction,
pubmed-meshheading:10671526-Spermatogenesis,
pubmed-meshheading:10671526-Spermatozoa,
pubmed-meshheading:10671526-Two-Hybrid System Techniques
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| pubmed:year |
2000
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| pubmed:articleTitle |
Binding and phosphorylation of a novel male germ cell-specific cGMP-dependent protein kinase-anchoring protein by cGMP-dependent protein kinase Ialpha.
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| pubmed:affiliation |
Discovery Research Laboratory, Tanabe Seiyaku Co. Ltd., 2-50 Kawagishi 2-chome, Toda, Saitama 335-8505, Japan.
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| pubmed:publicationType |
Journal Article
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