DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Eunjoon | ko |
dc.contributor.author | DeMarco, SJ | ko |
dc.contributor.author | Marfatia, SM | ko |
dc.contributor.author | Chishti, AH | ko |
dc.contributor.author | Sheng, M | ko |
dc.contributor.author | Strehler, EE | ko |
dc.date.accessioned | 2013-03-02T14:27:24Z | - |
dc.date.available | 2013-03-02T14:27:24Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1998-01 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.273, no.3, pp.1591 - 1595 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/73973 | - |
dc.description.abstract | 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. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | TUMOR-SUPPRESSOR PROTEIN | - |
dc.subject | NMDA RECEPTOR SUBUNITS | - |
dc.subject | CALCIUM-PUMP | - |
dc.subject | MONOCLONAL-ANTIBODIES | - |
dc.subject | MESSENGER-RNAS | - |
dc.subject | PSD-95 FAMILY | - |
dc.subject | HUMAN HOMOLOG | - |
dc.subject | RAT-BRAIN | - |
dc.subject | JUNCTIONS | - |
dc.subject | CELLS | - |
dc.title | Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains | - |
dc.type | Article | - |
dc.identifier.wosid | 000071411500047 | - |
dc.identifier.scopusid | 2-s2.0-0031594886 | - |
dc.type.rims | ART | - |
dc.citation.volume | 273 | - |
dc.citation.issue | 3 | - |
dc.citation.beginningpage | 1591 | - |
dc.citation.endingpage | 1595 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.273.3.1591 | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | DeMarco, SJ | - |
dc.contributor.nonIdAuthor | Marfatia, SM | - |
dc.contributor.nonIdAuthor | Chishti, AH | - |
dc.contributor.nonIdAuthor | Sheng, M | - |
dc.contributor.nonIdAuthor | Strehler, EE | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | TUMOR-SUPPRESSOR PROTEIN | - |
dc.subject.keywordPlus | NMDA RECEPTOR SUBUNITS | - |
dc.subject.keywordPlus | CALCIUM-PUMP | - |
dc.subject.keywordPlus | MONOCLONAL-ANTIBODIES | - |
dc.subject.keywordPlus | MESSENGER-RNAS | - |
dc.subject.keywordPlus | PSD-95 FAMILY | - |
dc.subject.keywordPlus | HUMAN HOMOLOG | - |
dc.subject.keywordPlus | RAT-BRAIN | - |
dc.subject.keywordPlus | JUNCTIONS | - |
dc.subject.keywordPlus | CELLS | - |
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