Analyses of Rem/RGK Signaling and Biological Activity

Douglas A. Andres; Shawn M. Crump; Robert N. Correll; Jonathan Satin; Brian S. Finlin

doi:10.1016/S0076-6879(05)07039-4

Analyses of Rem/RGK Signaling and Biological Activity

Douglas A. Andres, Shawn M. Crump, Robert N. Correll, Jonathan Satin, Brian S. Finlin

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

7 Scopus citations

Abstract

Rem (Rad and Gem related) is a member of the RGK family of Ras-related GTPases that also includes Rad, Rem2, and Gem/Kir. All RGK proteins share structural features that are distinct from other Ras-related proteins, including several nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains regulatory sites that seem to control both subcellular location and function. Rem is known to modulate two distinct signal transduction pathways, regulating both cytoskeletal reorganization and voltage-gated Ca²⁺ channel activity. In this chapter, we summarize the experimental approaches used to characterize the interaction of Rem with 14-3-3 proteins and Ca²⁺ channel β-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca²⁺ channel activity.

Original language	English
Pages (from-to)	484-498
Number of pages	15
Journal	Methods in Enzymology
Volume	407
DOIs	https://doi.org/10.1016/S0076-6879(05)07039-4
State	Published - 2006

Bibliographical note

Funding Information:
We acknowledge W. Peavler for his contributions to these studies. This work was supported in part by United States Public Health Service Grants HL‐072936 (D. A. A.) and HL‐074091 (J. S.), National Institutes of Health Grant P20RR0171 from the COBRE program of the NCRR (to D. A. A.), and by a Predoctoral Fellowship from the American Heart Association, Ohio Valley Affiliate (to R. N. C). J. S. is an Established Investigator of the American Heart Association.

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1016/S0076-6879(05)07039-4

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title = "Analyses of Rem/RGK Signaling and Biological Activity",

abstract = "Rem (Rad and Gem related) is a member of the RGK family of Ras-related GTPases that also includes Rad, Rem2, and Gem/Kir. All RGK proteins share structural features that are distinct from other Ras-related proteins, including several nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains regulatory sites that seem to control both subcellular location and function. Rem is known to modulate two distinct signal transduction pathways, regulating both cytoskeletal reorganization and voltage-gated Ca2+ channel activity. In this chapter, we summarize the experimental approaches used to characterize the interaction of Rem with 14-3-3 proteins and Ca2+ channel β-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca2+ channel activity.",

author = "Andres, {Douglas A.} and Crump, {Shawn M.} and Correll, {Robert N.} and Jonathan Satin and Finlin, {Brian S.}",

note = "Funding Information: We acknowledge W. Peavler for his contributions to these studies. This work was supported in part by United States Public Health Service Grants HL‐072936 (D. A. A.) and HL‐074091 (J. S.), National Institutes of Health Grant P20RR0171 from the COBRE program of the NCRR (to D. A. A.), and by a Predoctoral Fellowship from the American Heart Association, Ohio Valley Affiliate (to R. N. C). J. S. is an Established Investigator of the American Heart Association.",

year = "2006",

doi = "10.1016/S0076-6879(05)07039-4",

language = "English",

volume = "407",

pages = "484--498",

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T1 - Analyses of Rem/RGK Signaling and Biological Activity

AU - Andres, Douglas A.

AU - Crump, Shawn M.

AU - Correll, Robert N.

AU - Satin, Jonathan

AU - Finlin, Brian S.

N1 - Funding Information: We acknowledge W. Peavler for his contributions to these studies. This work was supported in part by United States Public Health Service Grants HL‐072936 (D. A. A.) and HL‐074091 (J. S.), National Institutes of Health Grant P20RR0171 from the COBRE program of the NCRR (to D. A. A.), and by a Predoctoral Fellowship from the American Heart Association, Ohio Valley Affiliate (to R. N. C). J. S. is an Established Investigator of the American Heart Association.

PY - 2006

Y1 - 2006

N2 - Rem (Rad and Gem related) is a member of the RGK family of Ras-related GTPases that also includes Rad, Rem2, and Gem/Kir. All RGK proteins share structural features that are distinct from other Ras-related proteins, including several nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains regulatory sites that seem to control both subcellular location and function. Rem is known to modulate two distinct signal transduction pathways, regulating both cytoskeletal reorganization and voltage-gated Ca2+ channel activity. In this chapter, we summarize the experimental approaches used to characterize the interaction of Rem with 14-3-3 proteins and Ca2+ channel β-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca2+ channel activity.

AB - Rem (Rad and Gem related) is a member of the RGK family of Ras-related GTPases that also includes Rad, Rem2, and Gem/Kir. All RGK proteins share structural features that are distinct from other Ras-related proteins, including several nonconservative amino acid substitutions within regions known to participate in nucleotide binding and hydrolysis and a C-terminal extension that contains regulatory sites that seem to control both subcellular location and function. Rem is known to modulate two distinct signal transduction pathways, regulating both cytoskeletal reorganization and voltage-gated Ca2+ channel activity. In this chapter, we summarize the experimental approaches used to characterize the interaction of Rem with 14-3-3 proteins and Ca2+ channel β-subunits and describe electrophysiological analyses for characterizing Rem-mediated regulation of L-type Ca2+ channel activity.

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DO - 10.1016/S0076-6879(05)07039-4

M3 - Review article

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AN - SCOPUS:33744516036

SN - 0076-6879

VL - 407

SP - 484

EP - 498

JO - Methods in Enzymology

JF - Methods in Enzymology

ER -

Analyses of Rem/RGK Signaling and Biological Activity

Abstract

Bibliographical note

ASJC Scopus subject areas

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