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

Eunjoon Kim, Steven J. DeMarco, Shirin M. Marfatia, Athar H. Chishti, Morgan Sheng, Emanuel E. Strehler

Research output: Contribution to journalArticle

134 Citations (Scopus)

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 Nmethyl-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 μM). 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.

Original languageEnglish (US)
Pages (from-to)1591-1595
Number of pages5
JournalJournal of Biological Chemistry
Volume273
Issue number3
DOIs
StatePublished - Jan 16 1998

Fingerprint

Guanylate Kinases
Calcium-Transporting ATPases
Cell membranes
Protein Isoforms
Cell Membrane
Alternative Splicing
Pumps
D-Aspartic Acid
Multiprotein Complexes
Peptides
Two-Hybrid System Techniques
Proteins
Surface Plasmon Resonance
COS Cells
Cluster Analysis
Homeostasis
Assays
Surface plasmon resonance
Yeast

ASJC Scopus subject areas

  • Biochemistry

Cite this

Plasma membrane Ca2+ ATPase isoform 4B binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains. / Kim, Eunjoon; DeMarco, Steven J.; Marfatia, Shirin M.; Chishti, Athar H.; Sheng, Morgan; Strehler, Emanuel E.

In: Journal of Biological Chemistry, Vol. 273, No. 3, 16.01.1998, p. 1591-1595.

Research output: Contribution to journalArticle

Kim, Eunjoon ; DeMarco, Steven J. ; Marfatia, Shirin M. ; Chishti, Athar H. ; Sheng, Morgan ; Strehler, Emanuel E. / Plasma membrane Ca2+ ATPase isoform 4B binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains. In: Journal of Biological Chemistry. 1998 ; Vol. 273, No. 3. pp. 1591-1595.
@article{e0fc5163d42a47158182d95f89cadceb,
title = "Plasma membrane Ca2+ ATPase isoform 4B binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains",
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 Nmethyl-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 μM). 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.",
author = "Eunjoon Kim and DeMarco, {Steven J.} and Marfatia, {Shirin M.} and Chishti, {Athar H.} and Morgan Sheng and Strehler, {Emanuel E.}",
year = "1998",
month = "1",
day = "16",
doi = "10.1074/jbc.273.3.1591",
language = "English (US)",
volume = "273",
pages = "1591--1595",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "3",

}

TY - JOUR

T1 - Plasma membrane Ca2+ ATPase isoform 4B binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains

AU - Kim, Eunjoon

AU - DeMarco, Steven J.

AU - Marfatia, Shirin M.

AU - Chishti, Athar H.

AU - Sheng, Morgan

AU - Strehler, Emanuel E.

PY - 1998/1/16

Y1 - 1998/1/16

N2 - 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 Nmethyl-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 μM). 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.

AB - 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 Nmethyl-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 μM). 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.

UR - http://www.scopus.com/inward/record.url?scp=0031594886&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031594886&partnerID=8YFLogxK

U2 - 10.1074/jbc.273.3.1591

DO - 10.1074/jbc.273.3.1591

M3 - Article

VL - 273

SP - 1591

EP - 1595

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 3

ER -