Multifactorial Regulation of G Protein-Coupled Receptor Endocytosis.
10.4062/biomolther.2016.186
- Author:
Xiaohan ZHANG
1
;
Kyeong Man KIM
Author Information
1. Pharmacology Laboratory, College of Pharmacy, Chonnam National University, Gwangju 61186, Republic of Korea. kmkim@jnu.ac.kr
- Publication Type:Review
- Keywords:
G protein-coupled receptor;
Endocytosis;
Ral;
ARF6;
Glycosylation;
Palmitoylation
- MeSH:
Binding Sites;
Cell Membrane;
Cooperative Behavior;
Endocytosis*;
Glycosylation;
Guanosine;
Humans;
Lipoylation;
Phosphorylation;
Protein Processing, Post-Translational
- From:Biomolecules & Therapeutics
2017;25(1):26-43
- CountryRepublic of Korea
- Language:English
-
Abstract:
Endocytosis is a process by which cells absorb extracellular materials via the inward budding of vesicles formed from the plasma membrane. Receptor-mediated endocytosis is a highly selective process where receptors with specific binding sites for extracellular molecules internalize via vesicles. G protein-coupled receptors (GPCRs) are the largest single family of plasma-membrane receptors with more than 1000 family members. But the molecular mechanisms involved in the regulation of GPCRs are believed to be highly conserved. For example, receptor phosphorylation in collaboration with β-arrestins plays major roles in desensitization and endocytosis of most GPCRs. Nevertheless, a number of subsequent studies showed that GPCR regulation, such as that by endocytosis, occurs through various pathways with a multitude of cellular components and processes. This review focused on i) functional interactions between homologous and heterologous pathways, ii) methodologies applied for determining receptor endocytosis, iii) experimental tools to determine specific endocytic routes, iv) roles of small guanosine triphosphate-binding proteins in GPCR endocytosis, and v) role of post-translational modification of the receptors in endocytosis.
