The calcium-sensing receptor and its interacting proteins: Ca2+ Sensing Receptor Review Series

Chunfa Huang, R. Tyler Miller

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Introduction Signalling by the Ca receptor Distinct effects of angiotensin II and Ca receptors Receptor activity modifying proteins (RAMPS) Filamin Potassium channels Other CaR-interacting proteins Conclusions Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling 'personalities'. The extracellular Ca-sensing receptor (CaR) signals via Gαi, Gαq and Gα12/13, but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling.

Original languageEnglish (US)
Pages (from-to)923-934
Number of pages12
JournalJournal of Cellular and Molecular Medicine
Volume11
Issue number5
DOIs
StatePublished - Sep 2007

Fingerprint

Receptor-Interacting Protein Serine-Threonine Kinases
Calcium-Sensing Receptors
Receptor Activity-Modifying Proteins
GTP-Binding Proteins
Filamins
Proteins
Potassium Channels
G-Protein-Coupled Receptors
Arrestins
Caveolins
Angiotensin Receptors
Monomeric GTP-Binding Proteins
Ubiquitination
Ion Channels
Angiotensin II
Personality
Membrane Proteins

Keywords

  • Calcium-sensing receptor
  • Cell signalling
  • Filamin channel
  • G protein-coupled receptor
  • Interaction
  • RAMP
  • Scaffold

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

The calcium-sensing receptor and its interacting proteins : Ca2+ Sensing Receptor Review Series. / Huang, Chunfa; Miller, R. Tyler.

In: Journal of Cellular and Molecular Medicine, Vol. 11, No. 5, 09.2007, p. 923-934.

Research output: Contribution to journalArticle

@article{3eca4a42a95a49838e3d302444cf918c,
title = "The calcium-sensing receptor and its interacting proteins: Ca2+ Sensing Receptor Review Series",
abstract = "Introduction Signalling by the Ca receptor Distinct effects of angiotensin II and Ca receptors Receptor activity modifying proteins (RAMPS) Filamin Potassium channels Other CaR-interacting proteins Conclusions Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling 'personalities'. The extracellular Ca-sensing receptor (CaR) signals via Gαi, Gαq and Gα12/13, but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling.",
keywords = "Calcium-sensing receptor, Cell signalling, Filamin channel, G protein-coupled receptor, Interaction, RAMP, Scaffold",
author = "Chunfa Huang and Miller, {R. Tyler}",
year = "2007",
month = "9",
doi = "10.1111/j.1582-4934.2007.00114.x",
language = "English (US)",
volume = "11",
pages = "923--934",
journal = "Journal of Cellular and Molecular Medicine",
issn = "1582-1838",
publisher = "Wiley-Blackwell",
number = "5",

}

TY - JOUR

T1 - The calcium-sensing receptor and its interacting proteins

T2 - Ca2+ Sensing Receptor Review Series

AU - Huang, Chunfa

AU - Miller, R. Tyler

PY - 2007/9

Y1 - 2007/9

N2 - Introduction Signalling by the Ca receptor Distinct effects of angiotensin II and Ca receptors Receptor activity modifying proteins (RAMPS) Filamin Potassium channels Other CaR-interacting proteins Conclusions Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling 'personalities'. The extracellular Ca-sensing receptor (CaR) signals via Gαi, Gαq and Gα12/13, but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling.

AB - Introduction Signalling by the Ca receptor Distinct effects of angiotensin II and Ca receptors Receptor activity modifying proteins (RAMPS) Filamin Potassium channels Other CaR-interacting proteins Conclusions Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling 'personalities'. The extracellular Ca-sensing receptor (CaR) signals via Gαi, Gαq and Gα12/13, but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling.

KW - Calcium-sensing receptor

KW - Cell signalling

KW - Filamin channel

KW - G protein-coupled receptor

KW - Interaction

KW - RAMP

KW - Scaffold

UR - http://www.scopus.com/inward/record.url?scp=35649001988&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35649001988&partnerID=8YFLogxK

U2 - 10.1111/j.1582-4934.2007.00114.x

DO - 10.1111/j.1582-4934.2007.00114.x

M3 - Article

C2 - 17979874

AN - SCOPUS:35649001988

VL - 11

SP - 923

EP - 934

JO - Journal of Cellular and Molecular Medicine

JF - Journal of Cellular and Molecular Medicine

SN - 1582-1838

IS - 5

ER -