The RGK family of GTP-binding proteins: Regulators of voltage-dependent calcium channels and cytoskeleton remodeling

Robert N. Correll; Chunyan Pang; Dana M. Niedowicz; Brian S. Finlin; Douglas A. Andres

doi:10.1016/j.cellsig.2007.10.028

The RGK family of GTP-binding proteins: Regulators of voltage-dependent calcium channels and cytoskeleton remodeling

Robert N. Correll, Chunyan Pang, Dana M. Niedowicz, Brian S. Finlin, Douglas A. Andres

Research output: Contribution to journal › Review article › peer-review

92 Scopus citations

Abstract

RGK proteins constitute a novel subfamily of small Ras-related proteins that function as potent inhibitors of voltage-dependent (VDCC) Ca²⁺ channels and regulators of actin cytoskeletal dynamics. Within the larger Ras superfamily, RGK proteins have distinct regulatory and structural characteristics, including nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains conserved regulatory sites which control both subcellular localization and function. RGK GTPases interact with the VDCC β-subunit (Ca_Vβ) and inhibit Rho/Rho kinase signaling to regulate VDCC activity and the cytoskeleton respectively. Binding of both calmodulin and 14-3-3 to RGK proteins, and regulation by phosphorylation controls cellular trafficking and the downstream signaling of RGK proteins, suggesting that a complex interplay between interacting protein factors and trafficking contribute to their regulation.

Original language	English
Pages (from-to)	292-300
Number of pages	9
Journal	Cellular Signalling
Volume	20
Issue number	2
DOIs	https://doi.org/10.1016/j.cellsig.2007.10.028
State	Published - Feb 2008

Bibliographical note

Funding Information:
We apologize to the scientists whose work was not cited due to space constraints. Research of the authors was supported by Public Health Service Grants HL072936 (to D.A.A.), a National Center for Research Resources grant P20 RR20171 (to D.A.A.), an American Diabetes Junior Faculty Award 7-05-JF-16 to (B.S.F.), and an NIH Interdisciplinary Cardiovascular Training Grant T32 HL072743 (to R.N.C.).

Keywords

Actin cytoskeleton
CaV1.2
Calcium
GTP-binding
Gem
Ion channel
Rad
Ras GTPase
Rem
Rem2
Signal transduction
VDCC

ASJC Scopus subject areas

Cell Biology

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10.1016/j.cellsig.2007.10.028

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title = "The RGK family of GTP-binding proteins: Regulators of voltage-dependent calcium channels and cytoskeleton remodeling",

abstract = "RGK proteins constitute a novel subfamily of small Ras-related proteins that function as potent inhibitors of voltage-dependent (VDCC) Ca2+ channels and regulators of actin cytoskeletal dynamics. Within the larger Ras superfamily, RGK proteins have distinct regulatory and structural characteristics, including nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains conserved regulatory sites which control both subcellular localization and function. RGK GTPases interact with the VDCC β-subunit (CaVβ) and inhibit Rho/Rho kinase signaling to regulate VDCC activity and the cytoskeleton respectively. Binding of both calmodulin and 14-3-3 to RGK proteins, and regulation by phosphorylation controls cellular trafficking and the downstream signaling of RGK proteins, suggesting that a complex interplay between interacting protein factors and trafficking contribute to their regulation.",

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author = "Correll, {Robert N.} and Chunyan Pang and Niedowicz, {Dana M.} and Finlin, {Brian S.} and Andres, {Douglas A.}",

note = "Funding Information: We apologize to the scientists whose work was not cited due to space constraints. Research of the authors was supported by Public Health Service Grants HL072936 (to D.A.A.), a National Center for Research Resources grant P20 RR20171 (to D.A.A.), an American Diabetes Junior Faculty Award 7-05-JF-16 to (B.S.F.), and an NIH Interdisciplinary Cardiovascular Training Grant T32 HL072743 (to R.N.C.). ",

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AU - Niedowicz, Dana M.

AU - Finlin, Brian S.

AU - Andres, Douglas A.

N1 - Funding Information: We apologize to the scientists whose work was not cited due to space constraints. Research of the authors was supported by Public Health Service Grants HL072936 (to D.A.A.), a National Center for Research Resources grant P20 RR20171 (to D.A.A.), an American Diabetes Junior Faculty Award 7-05-JF-16 to (B.S.F.), and an NIH Interdisciplinary Cardiovascular Training Grant T32 HL072743 (to R.N.C.).

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Y1 - 2008/2

N2 - RGK proteins constitute a novel subfamily of small Ras-related proteins that function as potent inhibitors of voltage-dependent (VDCC) Ca2+ channels and regulators of actin cytoskeletal dynamics. Within the larger Ras superfamily, RGK proteins have distinct regulatory and structural characteristics, including nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains conserved regulatory sites which control both subcellular localization and function. RGK GTPases interact with the VDCC β-subunit (CaVβ) and inhibit Rho/Rho kinase signaling to regulate VDCC activity and the cytoskeleton respectively. Binding of both calmodulin and 14-3-3 to RGK proteins, and regulation by phosphorylation controls cellular trafficking and the downstream signaling of RGK proteins, suggesting that a complex interplay between interacting protein factors and trafficking contribute to their regulation.

AB - RGK proteins constitute a novel subfamily of small Ras-related proteins that function as potent inhibitors of voltage-dependent (VDCC) Ca2+ channels and regulators of actin cytoskeletal dynamics. Within the larger Ras superfamily, RGK proteins have distinct regulatory and structural characteristics, including nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains conserved regulatory sites which control both subcellular localization and function. RGK GTPases interact with the VDCC β-subunit (CaVβ) and inhibit Rho/Rho kinase signaling to regulate VDCC activity and the cytoskeleton respectively. Binding of both calmodulin and 14-3-3 to RGK proteins, and regulation by phosphorylation controls cellular trafficking and the downstream signaling of RGK proteins, suggesting that a complex interplay between interacting protein factors and trafficking contribute to their regulation.

KW - Actin cytoskeleton

KW - CaV1.2

KW - Calcium

KW - GTP-binding

KW - Gem

KW - Ion channel

KW - Rad

KW - Ras GTPase

KW - Rem

KW - Rem2

KW - Signal transduction

KW - VDCC

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U2 - 10.1016/j.cellsig.2007.10.028

DO - 10.1016/j.cellsig.2007.10.028

M3 - Review article

C2 - 18042346

AN - SCOPUS:37549054055

SN - 0898-6568

VL - 20

SP - 292

EP - 300

JO - Cellular Signalling

JF - Cellular Signalling

IS - 2

ER -

The RGK family of GTP-binding proteins: Regulators of voltage-dependent calcium channels and cytoskeleton remodeling

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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