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protein kinase, cAMP-dependent, catalytic, alpha OKDB#: 4709
 Symbols: PRKACA Species: human
 Synonyms: PKACA, MGC48865, MGC102831,  Locus: 19p13.1 in Homo sapiens


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General Comment NCBI Summary: cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
General function Intracellular signaling cascade
Comment
Cellular localization Cytoplasmic, Plasma membrane
Comment
Ovarian function
Comment
Expression regulated by
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Ovarian localization Oocyte
Comment Analyses of the Involvement of PKA Regulation Mechanism in Meiotic Incompetence of Porcine Growing Oocytes. Nishimura T et al. Mammalian growing oocytes (GOs) lack an ability to resume meiosis, although the molecular mechanism of this limitation has not been fully understood. In the present study, we cloned cDNAs of cAMP-dependent protein-kinase (PKA) subunits from porcine oocytes, and analyzed the involvement of the PKA regulation mechanism in the meiotic incompetence of GOs at a molecular level. First, we found a cAMP-independent high PKA activity in GOs throughout the in vitro culture using the porcine-PKA assay system we established, and inhibition of the activity by injection of the antisense RNA of the PKA catalytic subunit (PKA-C) induced meiotic resumption in GOs. Then we examined the possibility that the amount of the PKA regulatory subunit (PKA-R), which bound and inhibited PKA-C, was insufficient to suppress PKA activity in GOs by overexpression of two PKA-Rs, PRKAR1A and PRKAR2A. We found that neither of them affected PKA activity and induced meiotic resumption in GO, while PRKAR2A could inhibit PKA activity and induce meiosis in cAMP-treated full-grown-oocytes (FGOs). Finally, we analyzed the subcellular localization of PKA subunits, and found that all subunits were localized in the cytoplasm during meiotic arrest and that PKA-C and PRKAR2A, but not PRKAR1A, entered into the nucleus just before meiotic resumption in FGO, whereas all of them remained at cytoplasm in GOs throughout the culture period. Our findings suggest that the continuous high PKA activity is a primary cause of the meiotic incompetence of porcine GOs, and that this PKA activity is not simply caused by an insufficient expression level of PKA-R, but can be attributed to more complex spatial-temporal regulation mechanisms.
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created: June 13, 2012, 12:37 p.m. by: hsueh   email:
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last update: June 13, 2012, 12:39 p.m. by: hsueh    email:



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