The DOI matches its Crossref record; 201 of the 201 references it cites were found in a registry or an index.
Regulation of GPCR activity, trafficking and localization by GPCR‐interacting proteins
Open accessAbstract
GPCRs represent the largest family of integral membrane proteins and were first identified as receptor proteins that couple via heterotrimeric G‐proteins to regulate a vast variety of effector proteins to modulate cellular function. It is now recognized that GPCRs interact with a myriad of proteins that not only function to attenuate their signalling but also function to couple these receptors to heterotrimeric G‐protein‐independent signalling pathways. In addition, intracellular and transmembrane proteins associate with GPCRs and regulate their processing in the endoplasmic reticulum, trafficking to the cell surface, compartmentalization to plasma membrane microdomains, endocytosis and trafficking between intracellular membrane compartments. The present review will overview the functional consequence of β‐arrestin, receptor activity‐modifying proteins (RAMPS), regulators of G‐protein signalling (RGS), GPCR‐associated sorting proteins (GASPs), Homer, small GTPases, PSD95/Disc Large/Zona Occludens (PDZ), spinophilin, protein phosphatases, calmodulin, optineurin and Src homology 3 (SH3) containing protein interactions with GPCRs. LINKED ARTICLES This article is part of a themed section on the Molecular Pharmacology of G Protein‐Coupled Receptors (GPCRs). To view the other articles in this section visit http://dx.doi.org/10.1111/bph.2012.165.issue‐6. To view the 2010 themed section on the same topic visit http://onlinelibrary.wiley.com/doi/10.1111/bph.2010.159.issue‐5/issuetoc
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Metadata
- Authors
- Magalhaes, A. C., Dunn, H., & Ferguson, S. S.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2012-02-22
- Volume
- 165
- Issue
- 6
- Pages
- 1717-1736
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- OpenAlex
- W2116265895
- Cited by
- 353
- References
- 201
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- bronze
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