Evidence map›Paper›PMID 32749217›Full record

ArticleeLife2020

Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1.

Marina Schrecker, Julia Korobenko, Richard K Hite

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

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  18. Lysosomal biogenesis and function in osteoclasts: a comprehensive review.Frontiers in cell and developmental biology · 2024
    Review
  19. Article
  20. Distinct ClC-6 and ClC-7 ClThe Journal of physiology · 2023
    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.

Marina SchreckerStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, United States.ORCID 0000-0001-8542-6657
Julia KorobenkoStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, United States.
Richard K HiteStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, United States.ORCID 0000-0003-0496-0669
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NCI NIH HHS P30 CA008748NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103310NIH HHS S10 OD019994
6 · The paper itself

Abstract

The chloride-proton exchanger CLC-7 plays critical roles in lysosomal homeostasis and bone regeneration and its mutation can lead to osteopetrosis, lysosomal storage disease and neurological disorders. In lysosomes and the ruffled border of osteoclasts, CLC-7 requires a β-subunit, OSTM1, for stability and activity. Here, we present electron cryomicroscopy structures of CLC-7 in occluded states by itself and in complex with OSTM1, determined at resolutions up to 2.8 Å. In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen. OSTM1 binding does not induce large-scale rearrangements of CLC-7, but does have minor effects on the conformation of the ion-conduction pathway, potentially contributing to its regulatory role. These studies provide insights into the role of OSTM1 and serve as a foundation for understanding the mechanisms of CLC-7 regulation.

Indexed as

Chloride ChannelsMembrane ProteinsUbiquitin-Protein LigasesAnimalsChickensCryoelectron MicroscopyHEK293 CellsHumansLysosomesMolecular Dynamics SimulationRecombinant ProteinsChloride ChannelsCLCN7 protein, humanMembrane ProteinsOSTM1 protein, humanRecombinant ProteinsUbiquitin-Protein Ligaseschloride transportCLChumanmolecular biophysicsproton transportstructural biology

Identifiers

PMID32749217
PMCPMC7440919
OpenAlexW3047453426

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.