IMR Press / FBL / Volume 22 / Issue 9 / DOI: 10.2741/4552

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Review

Endocytosis and membrane receptor internalization: implication of F-BAR protein Carom

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1 Center Department of Cardiology, Second Affiliated Hospital of Nanchang University, Nan Chang, Jiang Xi, 330006, China
2 Center for Metabolic Disease Research, Temple University School of Medicine, Philadelphia, PA, 19140, USA
3 Cardiovascular Research, Temple University School of Medicine, Philadelphia, PA, 19140, USA
4 Thrombosis Research, Temple University School of Medicine, Philadelphia, PA, 19140, USA
5 Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA, 19140, USA
6 Department of Cardiology, Changhai Hospital, Second Military Medical University, Shanghai, 200433, China
7 Department of Orthopedics, Second Affiliated Hospital of Nanchang University, Nan Chang, Jiang Xi, 330006, China

Academic Editor: Xiao-Feng Yang

Front. Biosci. (Landmark Ed) 2017, 22(9), 1439–1457; https://doi.org/10.2741/4552
Published: 1 March 2017
(This article belongs to the Special Issue CREG promotes vasculogenesis by activation of VEGFPI3KAkt pathway)
Abstract

Endocytosis is a cellular process mostly responsible for membrane receptor internalization. Cell membrane receptors bind to their ligands and form a complex which can be internalized. We previously proposed that F-BAR protein initiates membrane curvature and mediates endocytosis via its binding partners. However, F-BAR protein partners involved in membrane receptor endocytosis and the regulatory mechanism remain unknown. In this study, we established database mining strategies to explore mechanisms underlying receptor-related endocytosis. We identified 34 endocytic membrane receptors and 10 regulating proteins in clathrin-dependent endocytosis (CDE), a major process of membrane receptor internalization. We found that F-BAR protein FCHSD2 (Carom) may facilitate endocytosis via 9 endocytic partners. Carom is highly expressed, along with highly expressed endocytic membrane receptors and partners, in endothelial cells and macrophages. We established 3 models of Carom-receptor complexes and their intracellular trafficking based on protein interaction and subcellular localization. We conclude that Carom may mediate receptor endocytosis and transport endocytic receptors to the cytoplasm for receptor signaling and lysosome/proteasome degradation, or to the nucleus for RNA processing, gene transcription and DNA repair.

Keywords
F-BAR proteins
Membrane receptor
Cellular trafficking
Nuclear translocation
Endocytosis
Review
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