Linked Life Data

12511555

Source:http://linkedlifedata.com/resource/pubmed/id/12511555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2003-3-10
pubmed:abstractText
Spatial and temporal regulation of intracellular Ca(2+) is a key event in many signaling pathways. Plasma membrane Ca(2+)-ATPases (PMCAs) are major regulators of Ca(2+) homeostasis and bind to PDZ (PSD-95/Dlg/ZO-1) domains via their C termini. Various membrane-associated guanylate kinase family members have been identified as interaction partners of PMCAs. In particular, SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bind to the C-terminal tails of PMCA "b" splice variants. Additionally, it has been demonstrated that PMCA4b interacts with neuronal nitric-oxide synthase and that isoform 2b interacts with Na(+)/H(+) exchanger regulatory factor 2, both via a PDZ domain. CASK (calcium/calmodulin-dependent serine protein kinase) contains a calmodulin-dependent protein kinase-like domain followed by PDZ, SH3, and guanylate kinase-like domains. In adult brain CASK is located at neuronal synapses and interacts with various proteins, e.g. neurexin and Veli/LIN-7. In kidney it is localized to renal epithelia. Surprisingly, interaction with the Tbr-1 transcription factor, nuclear transport, binding to DNA T-elements (in a complex with Tbr-1), and transcriptional competence has been shown. Here we show that the C terminus of PMCA4b binds to CASK and that both proteins co-precipitate from brain and kidney tissue lysates. Immunofluorescence staining revealed co-expression of PMCA, CASK, and calbindin-d-28K in distal tubuli of rat kidney sections. To test if physical interaction of both proteins results in functional consequences we constructed a T-element-dependent reporter vector and investigated luciferase activity in HEK293 lysates, previously co-transfected with PMCA4b expression and control vectors. Expression of wild-type PMCA resulted in an 80% decrease in T-element-dependent transcriptional activity, whereas co-expression of a point-mutated PMCA, with nearly eliminated Ca(2+) pumping activity, had only a small influence on regulation of transcriptional activity. These results provide evidence of a new direct Ca(2+)-dependent link from the plasma membrane to the nucleus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9778-83
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12511555-Animals, pubmed-meshheading:12511555-Blotting, Western, pubmed-meshheading:12511555-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:12511555-Calcium-Transporting ATPases, pubmed-meshheading:12511555-Cation Transport Proteins, pubmed-meshheading:12511555-Cell Membrane, pubmed-meshheading:12511555-Cell Nucleus, pubmed-meshheading:12511555-Down-Regulation, pubmed-meshheading:12511555-Enzyme Inhibitors, pubmed-meshheading:12511555-Genetic Vectors, pubmed-meshheading:12511555-Guanylate Kinase, pubmed-meshheading:12511555-Humans, pubmed-meshheading:12511555-Immunohistochemistry, pubmed-meshheading:12511555-Kidney, pubmed-meshheading:12511555-Luciferases, pubmed-meshheading:12511555-Microscopy, Fluorescence, pubmed-meshheading:12511555-Nephrons, pubmed-meshheading:12511555-Nucleoside-Phosphate Kinase, pubmed-meshheading:12511555-Plasma Membrane Calcium-Transporting ATPases, pubmed-meshheading:12511555-Precipitin Tests, pubmed-meshheading:12511555-Protein Binding, pubmed-meshheading:12511555-Protein Isoforms, pubmed-meshheading:12511555-Protein Structure, Tertiary, pubmed-meshheading:12511555-Rats, pubmed-meshheading:12511555-Transfection
pubmed:year
2003
pubmed:articleTitle
Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK.
pubmed:affiliation
Department of Medicine, University of Wuerzburg, D-97080 Wuerzburg, Germany.
pubmed:publicationType
Journal Article