English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes

MPS-Authors
/persons/resource/persons207941

El Far,  O.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

/persons/resource/persons118039

Betz,  H.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

El Far, O., & Betz, H. (2002). G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes. Biochemical Journal, 365, 329-336.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-1C27-E
Abstract
G-protein-coupled receptors (GPCRs) represent a superfamily of highly diverse integral membrane proteins that transduce external signals to different subcellular compartments, including nuclei, via trimeric G-proteins. By differential activation of diffusible Galpha and membrane-bound Gbetagamma subunits, GPCRs might act on both cytoplasmic/intracellular and plasma-membrane-bound effector systems. The coupling efficiency and the plasma membrane localization of GPCRs are regulated by a variety of interacting proteins. In this review, we discuss recently disclosed protein interactions found with the cytoplasmic C-terminal tail regions of two types of presynaptic neurotransmitter receptors, the group III metabotropic glutamate receptors and the gamma-aminobutyric acid type-B receptors (GABA(B)Rs). Calmodulin binding to mGluR7 and other group III mGluRs may provide a Ca2+-dependent switch for unidirectional (Galpha) versus bidirectional (Galpha and Gbetagamma) signalling to downstream effector proteins. In addition, clustering of mGluR7 by PICK I (protein interacting with (C) under barC-(k) under bar inase (1) under bar), a polyspecific PDZ ((P) under bar SD-95/(D) under bar lg1/(Z) under barO-1) domain containing synaptic organizer protein, sheds light on how higher-order receptor complexes with regulatory enzymes (or 'signalosomes') could be formed. The interaction of GABA(B)Rs with the adaptor protein 14-3-3 and the transcription factor ATF4 ((a) under bar ctivating (t) under bar ranscription (f) under bar actor (4) under bar) suggests novel regulatory pathways for G-protein signalling, cytoskeletal reorganization and nuclear gene expression: processes that may all contribute to synaptic plasticity.