The closing and opening of TRPC channels by Homer1 and STIM1

Joseph P. Yuan, K. P. Lee, J. H. Hong, S. Muallem

Research output: Contribution to journalReview articleResearchpeer-review

47 Citations (Scopus)

Abstract

Influx of Ca 2+ is a central component of the receptor-evoked Ca 2+ signal. A ubiquitous form of Ca 2+ influx comes from Ca 2+ channels that are activated in response to depletion of the endoplasmic reticulum Ca 2+ stores and are thus named the store-operated Ca 2+-influx channels (SOCs). One form of SOC is the transient receptor potential canonical (TRPC) channels. A major question in the field of Ca 2+ signalling is the molecular mechanism that regulates the opening and closing of these channels. All TRPC channels have a Homer-binding ligand and two conserved negative charges that interact with two terminal lysines of the stromal interacting molecule 1 (STIM1). The Homer and STIM1 sites are separated by only four amino acid residues. Based on available results, we propose a molecular mechanism by which Homer couples TRPC channels to IP 3 receptors (IP 3Rs) to keep these channels in the closed state. Dissociation of the TRPCs-Homer-IP 3Rs complex allows STIM1 access to the TRPC channels negative charges to gate open these channels.

Original languageEnglish
Pages (from-to)238-247
Number of pages10
JournalActa Physiologica
Volume204
Issue number2
DOIs
StatePublished - 1 Feb 2012

Fingerprint

Transient Receptor Potential Channels
Endoplasmic Reticulum
Lysine
Ligands
Amino Acids

Keywords

  • Ca influx
  • Homer1
  • STIM1

Cite this

Yuan, Joseph P. ; Lee, K. P. ; Hong, J. H. ; Muallem, S. / The closing and opening of TRPC channels by Homer1 and STIM1. In: Acta Physiologica. 2012 ; Vol. 204, No. 2. pp. 238-247.
@article{28dcd40c355b4457afe285edebea3175,
title = "The closing and opening of TRPC channels by Homer1 and STIM1",
abstract = "Influx of Ca 2+ is a central component of the receptor-evoked Ca 2+ signal. A ubiquitous form of Ca 2+ influx comes from Ca 2+ channels that are activated in response to depletion of the endoplasmic reticulum Ca 2+ stores and are thus named the store-operated Ca 2+-influx channels (SOCs). One form of SOC is the transient receptor potential canonical (TRPC) channels. A major question in the field of Ca 2+ signalling is the molecular mechanism that regulates the opening and closing of these channels. All TRPC channels have a Homer-binding ligand and two conserved negative charges that interact with two terminal lysines of the stromal interacting molecule 1 (STIM1). The Homer and STIM1 sites are separated by only four amino acid residues. Based on available results, we propose a molecular mechanism by which Homer couples TRPC channels to IP 3 receptors (IP 3Rs) to keep these channels in the closed state. Dissociation of the TRPCs-Homer-IP 3Rs complex allows STIM1 access to the TRPC channels negative charges to gate open these channels.",
keywords = "Ca influx, Homer1, STIM1",
author = "Yuan, {Joseph P.} and Lee, {K. P.} and Hong, {J. H.} and S. Muallem",
year = "2012",
month = "2",
day = "1",
doi = "10.1111/j.1748-1716.2011.02319.x",
language = "English",
volume = "204",
pages = "238--247",
journal = "Acta Physiologica",
issn = "1748-1708",
publisher = "John Wiley and Sons Ltd",
number = "2",

}

The closing and opening of TRPC channels by Homer1 and STIM1. / Yuan, Joseph P.; Lee, K. P.; Hong, J. H.; Muallem, S.

In: Acta Physiologica, Vol. 204, No. 2, 01.02.2012, p. 238-247.

Research output: Contribution to journalReview articleResearchpeer-review

TY - JOUR

T1 - The closing and opening of TRPC channels by Homer1 and STIM1

AU - Yuan, Joseph P.

AU - Lee, K. P.

AU - Hong, J. H.

AU - Muallem, S.

PY - 2012/2/1

Y1 - 2012/2/1

N2 - Influx of Ca 2+ is a central component of the receptor-evoked Ca 2+ signal. A ubiquitous form of Ca 2+ influx comes from Ca 2+ channels that are activated in response to depletion of the endoplasmic reticulum Ca 2+ stores and are thus named the store-operated Ca 2+-influx channels (SOCs). One form of SOC is the transient receptor potential canonical (TRPC) channels. A major question in the field of Ca 2+ signalling is the molecular mechanism that regulates the opening and closing of these channels. All TRPC channels have a Homer-binding ligand and two conserved negative charges that interact with two terminal lysines of the stromal interacting molecule 1 (STIM1). The Homer and STIM1 sites are separated by only four amino acid residues. Based on available results, we propose a molecular mechanism by which Homer couples TRPC channels to IP 3 receptors (IP 3Rs) to keep these channels in the closed state. Dissociation of the TRPCs-Homer-IP 3Rs complex allows STIM1 access to the TRPC channels negative charges to gate open these channels.

AB - Influx of Ca 2+ is a central component of the receptor-evoked Ca 2+ signal. A ubiquitous form of Ca 2+ influx comes from Ca 2+ channels that are activated in response to depletion of the endoplasmic reticulum Ca 2+ stores and are thus named the store-operated Ca 2+-influx channels (SOCs). One form of SOC is the transient receptor potential canonical (TRPC) channels. A major question in the field of Ca 2+ signalling is the molecular mechanism that regulates the opening and closing of these channels. All TRPC channels have a Homer-binding ligand and two conserved negative charges that interact with two terminal lysines of the stromal interacting molecule 1 (STIM1). The Homer and STIM1 sites are separated by only four amino acid residues. Based on available results, we propose a molecular mechanism by which Homer couples TRPC channels to IP 3 receptors (IP 3Rs) to keep these channels in the closed state. Dissociation of the TRPCs-Homer-IP 3Rs complex allows STIM1 access to the TRPC channels negative charges to gate open these channels.

KW - Ca influx

KW - Homer1

KW - STIM1

UR - http://www.scopus.com/inward/record.url?scp=84855340495&partnerID=8YFLogxK

U2 - 10.1111/j.1748-1716.2011.02319.x

DO - 10.1111/j.1748-1716.2011.02319.x

M3 - Review article

VL - 204

SP - 238

EP - 247

JO - Acta Physiologica

JF - Acta Physiologica

SN - 1748-1708

IS - 2

ER -