The plasma membrane Ca(2+)-ATPase: regulation by PSD-95/Dlg/Zo-1 scaffolds

Since its first characterization in the erythrocyte membrane the plasma membrane Ca(2+)-ATPase has been well-defined as a ubiquitous mechanism for the efflux of Ca(2+) from eukaryotic cells. With 4 isoforms and potentially 30 splice variants, defining the absolute physiological role of plasma membra...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 2010-06, Vol.42 (6), p.805-808
Main Authors: Kruger, Wade A, Monteith, Gregory R, Poronnik, Philip
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - metabolism
Animals
Calcium Signaling
Cell Membrane - enzymology
Disks Large Homolog 4 Protein
Feedback, Physiological
Guanylate Kinases
Humans
Intracellular Signaling Peptides and Proteins - metabolism
Isoenzymes - genetics
Isoenzymes - metabolism
Membrane Proteins - metabolism
Multiprotein Complexes
Phosphoproteins - metabolism
Plasma Membrane Calcium-Transporting ATPases - genetics
Plasma Membrane Calcium-Transporting ATPases - metabolism
Zonula Occludens-1 Protein
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Summary:Since its first characterization in the erythrocyte membrane the plasma membrane Ca(2+)-ATPase has been well-defined as a ubiquitous mechanism for the efflux of Ca(2+) from eukaryotic cells. With 4 isoforms and potentially 30 splice variants, defining the absolute physiological role of plasma membrane Ca(2+)-ATPase has been difficult and very limited due to the lack of effective blockers/antibodies and difficulties in measuring the activity of individual isoforms. This review highlights recent developments showing that specific plasma membrane Ca(2+)-ATPase isoforms are subject to dynamic regulation by PSD-95/Dlg/Zo-1 scaffold proteins. Such interactions support a new paradigm, that by serving as key players in multifunctional protein complexes, transporters can regulate other signalling processes independent of their primary ion pumping function.
ISSN:1878-5875
DOI:10.1016/j.biocel.2010.01.023