Direct Binding between Pre-S1 and TRP-like Domains in TRPP Channels Mediates Gating and Functional Regulation by PIP2.

Abstract:

:Transient receptor potential (TRP) channels are regulated by diverse stimuli comprising thermal, chemical, and mechanical modalities. They are also commonly regulated by phosphatidylinositol-4,5-bisphosphate (PIP2), with underlying mechanisms largely unknown. We here revealed an intramolecular interaction of the TRPP3 N and C termini (N-C) that is functionally essential. The interaction was mediated by aromatic Trp81 in pre-S1 domain and cationic Lys568 in TRP-like domain. Structure-function analyses revealed similar N-C interaction in TRPP2 as well as TRPM8/-V1/-C4 via highly conserved tryptophan and lysine/arginine residues. PIP2 bound to cationic residues in TRPP3, including K568, thereby disrupting the N-C interaction and negatively regulating TRPP3. PIP2 had similar negative effects on TRPP2. Interestingly, we found that PIP2 facilitates the N-C interaction in TRPM8/-V1, resulting in channel potentiation. The intramolecular N-C interaction might represent a shared mechanism underlying the gating and PIP2 regulation of TRP channels.

journal_name

Cell Rep

journal_title

Cell reports

authors

Zheng W,Cai R,Hofmann L,Nesin V,Hu Q,Long W,Fatehi M,Liu X,Hussein S,Kong T,Li J,Light PE,Tang J,Flockerzi V,Tsiokas L,Chen XZ

doi

10.1016/j.celrep.2018.01.042

subject

Has Abstract

pub_date

2018-02-06 00:00:00

pages

1560-1573

issue

6

issn

2211-1247

pii

S2211-1247(18)30074-3

journal_volume

22

pub_type

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