VMAT structures reveal exciting targets for drug development

Shimon Schuldiner; Lucy R Forrest

doi:10.1016/j.tips.2024.02.004

VMAT structures reveal exciting targets for drug development

Trends Pharmacol Sci. 2024 May;45(5):385-387. doi: 10.1016/j.tips.2024.02.004. Epub 2024 Feb 29.

Authors

Shimon Schuldiner¹, Lucy R Forrest²

Affiliations

¹ Department of Biological Chemistry, Institute of Life Sciences, Silberman Bldg. 1-513, Edmond J. Safra Campus, Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel. Electronic address: shimon.schuldiner@mail.huji.ac.il.
² Computational Structural Biology Section, 35 Convent Drive, Room 3D-991, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-8202, USA. Electronic address: lucy.forrest@nih.gov.

PMID: 38429134
DOI: 10.1016/j.tips.2024.02.004

Abstract

Vesicular monoamine transporter (VMAT)-2 has a crucial role in the neurotransmission of biogenic amines. Recently, Dalton et al., Pidathala et al., Wu et al., and Wang et al. individually reported cryo-electron microscopy (EM) structures of human VMAT2, offering opportunities for developing improved therapeutics and deep insights into the functioning of this protein.

Keywords: cryo-EM structure; neurotransmission; neurotransmitter transporter; synaptic vesicles.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Animals
Cryoelectron Microscopy*
Drug Development*
Humans
Vesicular Monoamine Transport Proteins* / antagonists & inhibitors
Vesicular Monoamine Transport Proteins* / metabolism

Substances

Vesicular Monoamine Transport Proteins
SLC18A2 protein, human