rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
16
|
pubmed:dateCreated |
1998-9-8
|
pubmed:abstractText |
A Ca2+-pump ATPase, similar to that in the endoplasmic reticulum, has been located on the outer membrane of rat liver nuclei. The effect of cAMP-dependent protein kinase (PKA) on nuclear Ca2+-ATPase (NCA) was studied by using purified rat liver nuclei. Treatment of isolated nuclei with the catalytic unit of PKA resulted in the phosphorylation of a 105-kDa band that was recognized by antibodies specific for sarcoplasmic reticulum Ca2+-ATPase type 2b. Partial purification and immunoblotting confirmed that the 105-kDa protein band phosphorylated by PKA is NCA. The stoichiometry of phosphorylation was 0.76 mol of phosphate incorporated/mol of partially purified enzyme. Measurement of ATP-dependent 45Ca2+ uptake into purified nuclei showed that PKA phosphorylation enhanced the Ca2+-pumping activity of NCA. We show that PKA phosphorylation of Ca2+-ATPase enhances the transport of 10-kDa fluorescent-labeled dextrans across the nuclear envelope. The findings reported in this paper are consistent with the notion that the crosstalk between the cAMP/PKA- and Ca2+-dependent signaling pathways identified at the cytoplasmic level extends to the nucleus. Furthermore, these data support a function for crosstalk in the regulation of calcium-dependent transport across the nuclear envelope.
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pubmed:commentsCorrections |
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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
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pubmed:month |
Aug
|
pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
95
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
9178-83
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
|
pubmed:year |
1998
|
pubmed:articleTitle |
cAMP-dependent protein kinase phosphorylates and activates nuclear Ca2+-ATPase.
|
pubmed:affiliation |
Laboratoire de Neurobiologie Moléculaire des Interactions Cellulaires, UPR 416 du Centre National de la Recherche Scientifique, 5 rue Blaise Pascal, 67084 Strasbourg, France.
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pubmed:publicationType |
Journal Article
|