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Cell Calcium. 2019 Nov 22;86:102107. doi: 10.1016/j.ceca.2019.102107. [Epub ahead of print]

Structural insights into group II TRP channels.

Author information

1
Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, United States; Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, United States. Electronic address: Michael.Fine@utsouthwestern.edu.
2
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, United States; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, United States. Electronic address: Xiaochun.Li@utsouthwestern.edu.
3
Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China. Electronic address: sdang@ust.hk.

Abstract

The seven members of the TRP channel superfamily are divided into two main groups with five members comprising group I (TRPC/V/M/N/A) and TRPML (TRP MucoLipin) and TRPP (TRP Polycystin) making up group II. Group II channels share a high sequence homology on their transmembrane domains and are distinct from group I members as they contain a large luminal/extracellular domain between transmembrane helix 1 (S1) and S2. Since 2016, there are more than ten research papers reporting various structures of group II channels by either cryo-EM or X-ray crystallography. These studies along with recent functional analysis by the other groups have considerably strengthened our knowledge on TRPML and TRPP channels. In this review, we summarize and discuss these reports providing molecular insights into the group II TRP channel family.

KEYWORDS:

Cryo-EM structure; Mucolipidosis; PKD; Polycystin; TRPML; TRPP

PMID:
31841954
DOI:
10.1016/j.ceca.2019.102107

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