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rdf:type |
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lifeskim:mentions |
umls-concept:C0001476,
umls-concept:C0007603,
umls-concept:C0033684,
umls-concept:C0597298,
umls-concept:C0608660,
umls-concept:C0900627,
umls-concept:C1145667,
umls-concept:C1333226,
umls-concept:C1420744,
umls-concept:C1514562,
umls-concept:C1705335,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
1998-2-12
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pubmed:abstractText |
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 (KD = 1.6 nM), whereas binding to PDZ3 was in the micromolar range (KD = 1.2 microM). 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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Phosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plasma Membrane...,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/discs large 1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-1 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1591-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9430700-Alternative Splicing,
pubmed-meshheading:9430700-Animals,
pubmed-meshheading:9430700-Binding Sites,
pubmed-meshheading:9430700-COS Cells,
pubmed-meshheading:9430700-Calcium-Transporting ATPases,
pubmed-meshheading:9430700-Cation Transport Proteins,
pubmed-meshheading:9430700-Drosophila Proteins,
pubmed-meshheading:9430700-Guanylate Kinase,
pubmed-meshheading:9430700-Insect Proteins,
pubmed-meshheading:9430700-Isoenzymes,
pubmed-meshheading:9430700-Kinetics,
pubmed-meshheading:9430700-Membrane Proteins,
pubmed-meshheading:9430700-Nerve Tissue Proteins,
pubmed-meshheading:9430700-Nucleoside-Phosphate Kinase,
pubmed-meshheading:9430700-Phosphoproteins,
pubmed-meshheading:9430700-Plasma Membrane Calcium-Transporting ATPases,
pubmed-meshheading:9430700-Tumor Suppressor Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
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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pubmed:affiliation |
Howard Hughes Medical Institute, Massachusetts General Hospital, Harvard Medical School, Boston 02114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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