Article (Scientific journals)
Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK.
Schuh, Kai; Uldrijan, Stjepan; Gambaryan, Stepan et al.
2003In The Journal of biological chemistry, 278 (11), p. 9778-83
Peer reviewed
 

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Keywords :
Animals; Blotting, Western; Calcium-Calmodulin-Dependent Protein Kinases; Calcium-Transporting ATPases/chemistry/metabolism; Cation Transport Proteins; Cell Membrane/metabolism; Cell Nucleus/metabolism; Down-Regulation; Enzyme Inhibitors/pharmacology; Genetic Vectors/metabolism; Guanylate Kinase; Humans; Immunohistochemistry; Kidney/metabolism; Luciferases/metabolism; Microscopy, Fluorescence; Nephrons/metabolism; Nucleoside-Phosphate Kinase/chemistry/metabolism; Plasma Membrane Calcium-Transporting ATPases; Precipitin Tests; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Rats; Transfection
Abstract :
[en] 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.
Disciplines :
Human health sciences: Multidisciplinary, general & others
Author, co-author :
Schuh, Kai
Uldrijan, Stjepan
Gambaryan, Stepan
Roethlein, Nicola
Neyses, Ludwig ;  University of Luxembourg > Research Office
Language :
English
Title :
Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK.
Publication date :
2003
Journal title :
The Journal of biological chemistry
ISSN :
0021-9258
Volume :
278
Issue :
11
Pages :
9778-83
Peer reviewed :
Peer reviewed
Available on ORBilu :
since 16 October 2014

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