Evidence map›Paper›PMID 29577631›Full record

ReviewThe FEBS journal2018

The regulatory mechanism of mammalian TRPMLs revealed by cryo-EM.

Philip Schmiege, Michael Fine, Xiaochun Li

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Role of TRP channels in lymphatic function.Frontiers in physiology · 2026
    Review
  2. Inter-Organellar CaCells · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Structural basis for PtdInsPNature communications · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Philip SchmiegeDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Michael FineDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Xiaochun LiDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
The University of Texas Southwestern Medical Center · US

Funding

RENAL CONTROL OF BODY COMPOSITION AND BLOOD PRESSURET32DK007257 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI BAUM, MICHEL GERARD, MOE, ORSON W · 1986 to 2021
$5.0M
Palmitoylation-dependent massive endocytosis (pMEND)R01HL119843 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI HILGEMANN, DONALD W · 2014 to 2021
$3.1M
NHLBI NIH HHS R01 HL119843NIDDK NIH HHS T32 DK007257
6 · The paper itself

Abstract

Transient receptor potential mucolipin (TRPML) channels are the most recently identified subfamily of TRP channels and have seen a surge of new reports revealing both structural and functional insight. In 2017, several groups published multiple conformations of TRPML channels using cryo-EM. Similar to other TRP channels, the ML subfamily consists of six transmembrane helices (S1-S6), and a pore region including S5, S6, and two pore helices (PH1 and PH2). However, these reports also reveal distinct structural characteristics of the ML subfamily. Asp residues within the luminal pore may function to control calcium/pH regulation. A synthetic agonist, ML-SA1, can bind to the pore region of TRPMLs to force a direct dilation of the lower gate. Finally, biophysical and electrophysiological characterizations reveal another natural agonist binding site in the unique domain of TRPMLs, presumably regulating the conformation of the S4-S5 linker to open the channel. This work elucidates the molecular architecture and provides insights into how multiple ligands regulate TRPMLs.

Indexed as

Binding SitesCryoelectron MicroscopyGene ExpressionHumansLysosomal Storage DiseasesLysosomesModels, MolecularPhosphatidylinositol PhosphatesPhthalimidesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsQuinolinesTransient Receptor Potential ChannelsTRPV Cation ChannelsMCOLN1 protein, humanMCOLN3 protein, humanML-SA1 compoundphosphatidylinositol 3,5-diphosphatePhosphatidylinositol PhosphatesPhthalimidesQuinolinesTransient Receptor Potential ChannelsTRPV1 protein, humanTRPV Cation Channelscryo-EMML-SA1pH regulationPIP 2TRPML

Identifiers

PMID29577631
PMCPMC6105560
OpenAlexW2789458000

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.