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CRIP1a inhibits endocytosis of G-protein coupled receptors activated by endocannabinoids and glutamate by a common molecular mechanism.
Mascia, Fabrizio; Klotz, Lisa; Lerch, Judith; Ahmed, Mostafa H; Zhang, Yan; Enz, Ralf.
Afiliación
  • Mascia F; Institut für Biochemie (Emil-Fischer-Zentrum), Universität Erlangen-Nürnberg, Erlangen, Germany.
  • Klotz L; Institut für Biochemie (Emil-Fischer-Zentrum), Universität Erlangen-Nürnberg, Erlangen, Germany.
  • Lerch J; Institut für Biochemie (Emil-Fischer-Zentrum), Universität Erlangen-Nürnberg, Erlangen, Germany.
  • Ahmed MH; Department of Medicinal Chemistry, Virginia Commonwealth University, Richmond, Virginia, USA.
  • Zhang Y; Department of Medicinal Chemistry, Virginia Commonwealth University, Richmond, Virginia, USA.
  • Enz R; Institut für Biochemie (Emil-Fischer-Zentrum), Universität Erlangen-Nürnberg, Erlangen, Germany.
J Neurochem ; 141(4): 577-591, 2017 05.
Article en En | MEDLINE | ID: mdl-28295323
The excitability of the central nervous system depends largely on the surface density of neurotransmitter receptors. The endocannabinoid receptor 1 (CB1 R) and the metabotropic glutamate receptor mGlu8 R are expressed pre-synaptically where they reduce glutamate release into the synaptic cleft. Recently, the CB1 R interacting protein cannabinoid receptor interacting protein 1a (CRIP1a) was identified and characterized to regulate CB1 R activity in neurons. However, underlying molecular mechanisms are largely unknown. Here, we identified a common mechanism used by CRIP1a to regulate the cell surface density of two different types of G-protein coupled receptors, CB1 R and mGlu8a R. Five amino acids within the CB1 R C-terminus were required and sufficient to reduce constitutive CB1 R endocytosis by about 72% in the presence of CRIP1a. Interestingly, a similar sequence is present in mGlu8a R and consistently, endocytosis of mGlu8a R depended on CRIP1a, as well. Docking analysis and molecular dynamics simulations identified a conserved serine in CB1 R (S468) and mGlu8a R (S894) that forms a hydrogen bond with the peptide backbone of CRIP1a at position R82. In contrast to mGlu8a R, the closely related mGlu8b R splice-variant carries a lysine (K894) at this position, and indeed, mGlu8b R endocytosis was not affected by CRIP1a. Chimeric constructs between CB1 R, mGlu8a R, and mGlu8b R underline the role of the identified five CRIP1a sensitive amino acids. In summary, we suggest that CRIP1a negatively regulates endocytosis of two different G-protein coupled receptor types, CB1 R and mGlu8a R.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Portadoras / Receptores Acoplados a Proteínas G / Endocannabinoides / Endocitosis / Moduladores de Receptores de Cannabinoides / Glutamatos Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Portadoras / Receptores Acoplados a Proteínas G / Endocannabinoides / Endocitosis / Moduladores de Receptores de Cannabinoides / Glutamatos Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido