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EH domain‐containing protein 2 (EHD2): Overview, biological function, and therapeutic potential.

Authors :
Zhu, Guoqiang
Zhang, Hu
Xia, Min
Liu, Yiqi
Li, Mingyong
Source :
Cell Biochemistry & Function. Apr2024, Vol. 42 Issue 3, p1-12. 12p.
Publication Year :
2024

Abstract

EH domain‐containing protein 2 (EHD2) is a member of the EHD protein family and is mainly located in the plasma membrane, but can also be found in the cytoplasm and endosomes. EHD2 is also a nuclear‐cytoplasmic shuttle protein. After entering the cell nuclear, EHD2 acts as a corepressor of transcription to inhibit gene transcription. EHD2 regulates a series of biological processes. As a key regulator of endocytic transport, EHD2 is involved in the formation and maintenance of endosomal tubules and vesicles, which are critical for the intracellular transport of proteins and other substances. The N‐terminal of EHD2 is attached to the cell membrane, while its C‐terminal binds to the actin‐binding protein. After binding, EHD2 connects with the actin cytoskeleton, forming the curvature of the membrane and promoting cell endocytosis. EHD2 is also associated with membrane protein trafficking and receptor signaling, as well as in glucose metabolism and lipid metabolism. In this review, we highlight the recent advances in the function of EHD2 in various cellular processes and its potential implications in human diseases such as cancer and metabolic disease. We also discussed the prospects for the future of EHD2. EHD2 has a broad prospect as a therapeutic target for a variety of diseases. Further research is needed to explore its mechanism, which could pave the way for the development of targeted treatments. Significance statement: The overview and biological function of EH domain‐containing protein 2 (EHD2) are discussed in this article.The article focuses on the role of EHD2 in metabolic diseases and cancer.The article also discussed the prospects for the future of EHD2 (Figure 1). [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
02636484
Volume :
42
Issue :
3
Database :
Academic Search Index
Journal :
Cell Biochemistry & Function
Publication Type :
Academic Journal
Accession number :
176868270
Full Text :
https://doi.org/10.1002/cbf.4016