Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains

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Plasma membrane Ca2+ ATPases are P-type pumps important for intracellular Ca2+ homeostasis. The extreme C termini of alternatively spliced "b"-type Ca2+ pump isoforms resemble those of K+ channels and N-methyl-D-aspartate receptor subunits that interact with channel-clustering proteins of the membrane-associated guanylate kinase (MAGUK) family via PDZ domains, Yeast two-hybrid assays demonstrated strong interaction of Ca2+ pump 4b with the PDZ1+2 domains of several mammalian MAGUKs. Pump 4b and PSD-95 could be co-immunoprecipitated from COS-7 cells overexpressing these proteins. Surface plasmon resonance revealed that a C-terminal pump 4b peptide interacted with the PDZ1+2 domains of hDlg with nanomolar affinity (K-D = 1.6 nm), whereas binding to PDZ3 was in the micromolar range (K-D = 1.2 mu M). In contrast, the corresponding C-terminal peptide of Ca2+ pump 2b interacted weakly with PDZ1+2 and not at all with PDZ3 of hDlg. Ca2+ pump 4b bound strongly to PDZ1+2+3 of hDlg on filter assays, whereas isoform 2b bound weakly, and the splice variants 2a and 4a failed to bind. Together, these data demonstrate a direct physical binding of Ca2+ pump isoform 4b to MAGUKs via their PDZ domains and reveal a novel role of alternative splicing within the family of plasma membrane Ca2+ pumps. Alternative splicing may dictate their specific interaction with PDZ domain-containing proteins, potentially influencing their localization and incorporation into functional multiprotein complexes at the plasma membrane.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
1998-01
Language
English
Article Type
Article
Keywords

TUMOR-SUPPRESSOR PROTEIN; NMDA RECEPTOR SUBUNITS; CALCIUM-PUMP; MONOCLONAL-ANTIBODIES; MESSENGER-RNAS; PSD-95 FAMILY; HUMAN HOMOLOG; RAT-BRAIN; JUNCTIONS; CELLS

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.273, no.3, pp.1591 - 1595

ISSN
0021-9258
DOI
10.1074/jbc.273.3.1591
URI
http://hdl.handle.net/10203/73973
Appears in Collection
BS-Journal Papers(저널논문)
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