Supramolecular assemblies and localized regulation of voltage-gated ion channels

Shuiping Dai; Duane D Hall; Johannes W Hell

doi:10.1152/physrev.00029.2007

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Supramolecular assemblies and localized regulation of voltage-gated ion channels

Journal article

Peer reviewed

Supramolecular assemblies and localized regulation of voltage-gated ion channels

Shuiping Dai, Duane D Hall and Johannes W Hell

Physiological reviews, Vol.89(2), pp.411-452

04/2009

DOI: 10.1152/physrev.00029.2007

PMCID: PMC2733249

PMID: 19342611

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Abstract

This review addresses the localized regulation of voltage-gated ion channels by phosphorylation. Comprehensive data on channel regulation by associated protein kinases, phosphatases, and related regulatory proteins are mainly available for voltage-gated Ca2+ channels, which form the main focus of this review. Other voltage-gated ion channels and especially Kv7.1-3 (KCNQ1-3), the large- and small-conductance Ca2+-activated K+ channels BK and SK2, and the inward-rectifying K+ channels Kir3 have also been studied to quite some extent and will be included. Regulation of the L-type Ca2+ channel Cav1.2 by PKA has been studied most thoroughly as it underlies the cardiac fight-or-flight response. A prototypical Cav1.2 signaling complex containing the beta2 adrenergic receptor, the heterotrimeric G protein Gs, adenylyl cyclase, and PKA has been identified that supports highly localized via cAMP. The type 2 ryanodine receptor as well as AMPA- and NMDA-type glutamate receptors are in close proximity to Cav1.2 in cardiomyocytes and neurons, respectively, yet independently anchor PKA, CaMKII, and the serine/threonine phosphatases PP1, PP2A, and PP2B, as is discussed in detail. Descriptions of the structural and functional aspects of the interactions of PKA, PKC, CaMKII, Src, and various phosphatases with Cav1.2 will include comparisons with analogous interactions with other channels such as the ryanodine receptor or ionotropic glutamate receptors. Regulation of Na+ and K+ channel phosphorylation complexes will be discussed in separate papers. This review is thus intended for readers interested in ion channel regulation or in localization of kinases, phosphatases, and their upstream regulators.

Cyclic AMP-Dependent Protein Kinases - physiology

Ion Channel Gating - physiology

Animals

Protein Kinase C - physiology

Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology

Humans

Ion Channels - physiology

src-Family Kinases - physiology

Phosphoprotein Phosphatases - physiology

Ion Channels - chemistry

Details

Title: Subtitle: Supramolecular assemblies and localized regulation of voltage-gated ion channels
Creators: Shuiping Dai - Department of Pharmacology, University of Iowa, Iowa City, IA 52242-1109, USA
Duane D Hall
Johannes W Hell
Resource Type: Journal article
Publication Details: Physiological reviews, Vol.89(2), pp.411-452
DOI: 10.1152/physrev.00029.2007
PMID: 19342611
PMCID: PMC2733249
NLM abbreviation: Physiol Rev
ISSN: 0031-9333
eISSN: 1522-1210
Grant note: R01-NS-35563 / NINDS NIH HHS R01 AG017502 / NIA NIH HHS R01 NS046450-04 / NINDS NIH HHS R01-AG-17502 / NIA NIH HHS R01 NS035563 / NINDS NIH HHS R01 NS035563-04 / NINDS NIH HHS R01 NS046450 / NINDS NIH HHS R01 AG017502-07 / NIA NIH HHS R01-NS-46450 / NINDS NIH HHS
Language: English
Date published: 04/2009
Academic Unit: Cardiovascular Medicine; Internal Medicine
Record Identifier: 9984094496202771

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