Plasma Membrane Ca2+-ATPase Isoforms 2b and 4b Interact Promiscuously and Selectively with Members of the Membrane-associated Guanylate Kinase Family of PDZ (PSD95/Dlg/ZO-1) Domain-containing Proteins

Steven J. DeMarco, Emanuel E. Strehler

Research output: Contribution to journalArticle

129 Citations (Scopus)

Abstract

Spatial and temporal regulation of intracellular Ca2+ signaling depends on localized Ca2+ microdomains containing the requisite molecular components for Ca2+ influx, efflux, and signal transmission. Plasma membrane Ca2+-ATPase (PMCA) isoforms of the "b" splice type contain predicted PDZ (PSD95/Dlg/ZO-1) interaction domains. The COOH-terminal tail of PMCA2b isolated the membrane-associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding partner in a yeast two-hybrid screen. The related MAGUKs SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bound to the COOH-terminal tail of PMCA4b, whereas only the first three bound to the tail of PMCA2b. Coimmunoprecipitations confirmed the interaction selectivity between PMCA4b and SAP102 as opposed to the promiscuity of PMCA2b and 4b in interacting with other SAPs. Confocal immunofluorescence microscopy revealed the exclusive presence and colocalization of PMCA4b and SAP97 in the basolateral membrane of polarized Madin-Darby canine kidney epithelial cells. In hippocampal neurons, PMCA2b was abundant throughout the somatodendritic compartment and often extended into the neck and head of individual spines where it colocalized with SAP90/PSD95. These data show that PMCA "b" splice forms interact promiscuously but also with specificity with different members of the PSD95 family of SAPs. PMCA-SAP interactions may play a role in the recruitment and maintenance of the PMCA at specific membrane domains involved in local Ca2+ regulation.

Original languageEnglish (US)
Pages (from-to)21594-21600
Number of pages7
JournalJournal of Biological Chemistry
Volume276
Issue number24
DOIs
StatePublished - Jun 15 2001

Fingerprint

Guanylate Kinases
Calcium-Transporting ATPases
Cell membranes
Protein Isoforms
Cell Membrane
Proteins
Membranes
Madin Darby Canine Kidney Cells
Confocal microscopy
Fluorescence Microscopy
Confocal Microscopy
Yeast
Neurons
Spine
Neck
Yeasts
Epithelial Cells
Maintenance
Protein Domains

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{0e4b992e452446b29494863af5aae541,
title = "Plasma Membrane Ca2+-ATPase Isoforms 2b and 4b Interact Promiscuously and Selectively with Members of the Membrane-associated Guanylate Kinase Family of PDZ (PSD95/Dlg/ZO-1) Domain-containing Proteins",
abstract = "Spatial and temporal regulation of intracellular Ca2+ signaling depends on localized Ca2+ microdomains containing the requisite molecular components for Ca2+ influx, efflux, and signal transmission. Plasma membrane Ca2+-ATPase (PMCA) isoforms of the {"}b{"} splice type contain predicted PDZ (PSD95/Dlg/ZO-1) interaction domains. The COOH-terminal tail of PMCA2b isolated the membrane-associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding partner in a yeast two-hybrid screen. The related MAGUKs SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bound to the COOH-terminal tail of PMCA4b, whereas only the first three bound to the tail of PMCA2b. Coimmunoprecipitations confirmed the interaction selectivity between PMCA4b and SAP102 as opposed to the promiscuity of PMCA2b and 4b in interacting with other SAPs. Confocal immunofluorescence microscopy revealed the exclusive presence and colocalization of PMCA4b and SAP97 in the basolateral membrane of polarized Madin-Darby canine kidney epithelial cells. In hippocampal neurons, PMCA2b was abundant throughout the somatodendritic compartment and often extended into the neck and head of individual spines where it colocalized with SAP90/PSD95. These data show that PMCA {"}b{"} splice forms interact promiscuously but also with specificity with different members of the PSD95 family of SAPs. PMCA-SAP interactions may play a role in the recruitment and maintenance of the PMCA at specific membrane domains involved in local Ca2+ regulation.",
author = "DeMarco, {Steven J.} and Strehler, {Emanuel E.}",
year = "2001",
month = "6",
day = "15",
doi = "10.1074/jbc.M101448200",
language = "English (US)",
volume = "276",
pages = "21594--21600",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "24",

}

TY - JOUR

T1 - Plasma Membrane Ca2+-ATPase Isoforms 2b and 4b Interact Promiscuously and Selectively with Members of the Membrane-associated Guanylate Kinase Family of PDZ (PSD95/Dlg/ZO-1) Domain-containing Proteins

AU - DeMarco, Steven J.

AU - Strehler, Emanuel E.

PY - 2001/6/15

Y1 - 2001/6/15

N2 - Spatial and temporal regulation of intracellular Ca2+ signaling depends on localized Ca2+ microdomains containing the requisite molecular components for Ca2+ influx, efflux, and signal transmission. Plasma membrane Ca2+-ATPase (PMCA) isoforms of the "b" splice type contain predicted PDZ (PSD95/Dlg/ZO-1) interaction domains. The COOH-terminal tail of PMCA2b isolated the membrane-associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding partner in a yeast two-hybrid screen. The related MAGUKs SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bound to the COOH-terminal tail of PMCA4b, whereas only the first three bound to the tail of PMCA2b. Coimmunoprecipitations confirmed the interaction selectivity between PMCA4b and SAP102 as opposed to the promiscuity of PMCA2b and 4b in interacting with other SAPs. Confocal immunofluorescence microscopy revealed the exclusive presence and colocalization of PMCA4b and SAP97 in the basolateral membrane of polarized Madin-Darby canine kidney epithelial cells. In hippocampal neurons, PMCA2b was abundant throughout the somatodendritic compartment and often extended into the neck and head of individual spines where it colocalized with SAP90/PSD95. These data show that PMCA "b" splice forms interact promiscuously but also with specificity with different members of the PSD95 family of SAPs. PMCA-SAP interactions may play a role in the recruitment and maintenance of the PMCA at specific membrane domains involved in local Ca2+ regulation.

AB - Spatial and temporal regulation of intracellular Ca2+ signaling depends on localized Ca2+ microdomains containing the requisite molecular components for Ca2+ influx, efflux, and signal transmission. Plasma membrane Ca2+-ATPase (PMCA) isoforms of the "b" splice type contain predicted PDZ (PSD95/Dlg/ZO-1) interaction domains. The COOH-terminal tail of PMCA2b isolated the membrane-associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding partner in a yeast two-hybrid screen. The related MAGUKs SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bound to the COOH-terminal tail of PMCA4b, whereas only the first three bound to the tail of PMCA2b. Coimmunoprecipitations confirmed the interaction selectivity between PMCA4b and SAP102 as opposed to the promiscuity of PMCA2b and 4b in interacting with other SAPs. Confocal immunofluorescence microscopy revealed the exclusive presence and colocalization of PMCA4b and SAP97 in the basolateral membrane of polarized Madin-Darby canine kidney epithelial cells. In hippocampal neurons, PMCA2b was abundant throughout the somatodendritic compartment and often extended into the neck and head of individual spines where it colocalized with SAP90/PSD95. These data show that PMCA "b" splice forms interact promiscuously but also with specificity with different members of the PSD95 family of SAPs. PMCA-SAP interactions may play a role in the recruitment and maintenance of the PMCA at specific membrane domains involved in local Ca2+ regulation.

UR - http://www.scopus.com/inward/record.url?scp=0035877655&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035877655&partnerID=8YFLogxK

U2 - 10.1074/jbc.M101448200

DO - 10.1074/jbc.M101448200

M3 - Article

C2 - 11274188

AN - SCOPUS:0035877655

VL - 276

SP - 21594

EP - 21600

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 24

ER -