14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity

Thomas Benzing, Michael B. Yaffe, Thierry Arnould, Lorenz Sellin, Bernhard Schermer, Birgit Schilling, Rainer Schreiber, Karl Kunzelmann, German G. Leparc, Emily Kim, Gerd Walz

Résultats de recherche: Contribution à un journal/une revueArticle

Résumé

Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) that stimulate the inactivation of heterotrimeric G proteins. We have recently shown that RGS proteins may be regulated on a post-translational level (Benzing, T., Brandes, R., Sellin, L., Schermer, B., Lecker, S., Walz, G., and Kim, E. (1999) Nat. Med. 5, 913-918). However, mechanisms controlling the GAP activity of RGS proteins are poorly understood. Here we show that 14-3-3 proteins associate with RGS7 and RGS3. Binding of 14-3-3 is mediated by a conserved phosphoserine located in the Gα-interacting portion of the RGS domain; interaction with 14-3-3 inhibits the GAP activity of RGS7, depends upon phosphorylation of a conserved residue within the RGS domain, and results in inhibition of GAP function. Collectively, these data indicate that phosphorylation-dependent binding of 14-3-3 may act as molecular switch that controls the GAP activity keeping a substantial fraction of RGS proteins in a dormant state.

langueAnglais
Pages28167-28172
Nombre de pages6
journalJ Biol Chem
Volume275
Numéro36
Les DOIs
étatPublié - 8 sept. 2000

Empreinte digitale

RGS Proteins
GTPase-Activating Proteins
GTP-Binding Proteins
Phosphorylation
Protein Domains
GTP-Binding Protein Regulators
14-3-3 Proteins
Phosphoserine
Heterotrimeric GTP-Binding Proteins
Switches

Citer ceci

Benzing, T., Yaffe, M. B., Arnould, T., Sellin, L., Schermer, B., Schilling, B., ... Walz, G. (2000). 14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity. J Biol Chem, 275(36), 28167-28172. DOI: 10.1074/jbc.M002905200
Benzing, Thomas ; Yaffe, Michael B. ; Arnould, Thierry ; Sellin, Lorenz ; Schermer, Bernhard ; Schilling, Birgit ; Schreiber, Rainer ; Kunzelmann, Karl ; Leparc, German G. ; Kim, Emily ; Walz, Gerd. / 14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity. Dans: J Biol Chem. 2000 ; Vol 275, Numéro 36. p. 28167-28172
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abstract = "Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) that stimulate the inactivation of heterotrimeric G proteins. We have recently shown that RGS proteins may be regulated on a post-translational level (Benzing, T., Brandes, R., Sellin, L., Schermer, B., Lecker, S., Walz, G., and Kim, E. (1999) Nat. Med. 5, 913-918). However, mechanisms controlling the GAP activity of RGS proteins are poorly understood. Here we show that 14-3-3 proteins associate with RGS7 and RGS3. Binding of 14-3-3 is mediated by a conserved phosphoserine located in the Gα-interacting portion of the RGS domain; interaction with 14-3-3 inhibits the GAP activity of RGS7, depends upon phosphorylation of a conserved residue within the RGS domain, and results in inhibition of GAP function. Collectively, these data indicate that phosphorylation-dependent binding of 14-3-3 may act as molecular switch that controls the GAP activity keeping a substantial fraction of RGS proteins in a dormant state.",
author = "Thomas Benzing and Yaffe, {Michael B.} and Thierry Arnould and Lorenz Sellin and Bernhard Schermer and Birgit Schilling and Rainer Schreiber and Karl Kunzelmann and Leparc, {German G.} and Emily Kim and Gerd Walz",
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Benzing, T, Yaffe, MB, Arnould, T, Sellin, L, Schermer, B, Schilling, B, Schreiber, R, Kunzelmann, K, Leparc, GG, Kim, E & Walz, G 2000, '14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity' J Biol Chem, VOL 275, Numéro 36, p. 28167-28172. DOI: 10.1074/jbc.M002905200

14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity. / Benzing, Thomas; Yaffe, Michael B.; Arnould, Thierry; Sellin, Lorenz; Schermer, Bernhard; Schilling, Birgit; Schreiber, Rainer; Kunzelmann, Karl; Leparc, German G.; Kim, Emily; Walz, Gerd.

Dans: J Biol Chem, Vol 275, Numéro 36, 08.09.2000, p. 28167-28172.

Résultats de recherche: Contribution à un journal/une revueArticle

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T1 - 14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity

AU - Benzing,Thomas

AU - Yaffe,Michael B.

AU - Arnould,Thierry

AU - Sellin,Lorenz

AU - Schermer,Bernhard

AU - Schilling,Birgit

AU - Schreiber,Rainer

AU - Kunzelmann,Karl

AU - Leparc,German G.

AU - Kim,Emily

AU - Walz,Gerd

PY - 2000/9/8

Y1 - 2000/9/8

N2 - Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) that stimulate the inactivation of heterotrimeric G proteins. We have recently shown that RGS proteins may be regulated on a post-translational level (Benzing, T., Brandes, R., Sellin, L., Schermer, B., Lecker, S., Walz, G., and Kim, E. (1999) Nat. Med. 5, 913-918). However, mechanisms controlling the GAP activity of RGS proteins are poorly understood. Here we show that 14-3-3 proteins associate with RGS7 and RGS3. Binding of 14-3-3 is mediated by a conserved phosphoserine located in the Gα-interacting portion of the RGS domain; interaction with 14-3-3 inhibits the GAP activity of RGS7, depends upon phosphorylation of a conserved residue within the RGS domain, and results in inhibition of GAP function. Collectively, these data indicate that phosphorylation-dependent binding of 14-3-3 may act as molecular switch that controls the GAP activity keeping a substantial fraction of RGS proteins in a dormant state.

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Benzing T, Yaffe MB, Arnould T, Sellin L, Schermer B, Schilling B et al. 14-3-3 Interacts with regulator of G protein signaling proteins and modulates their activity. J Biol Chem. 2000 sept. 8;275(36):28167-28172. Disponible �, DOI: 10.1074/jbc.M002905200