Evidence map›Paper›PMID 33964204›Full record

ArticleMolecular cell2021

WNK1 is an assembly factor for the human ER membrane protein complex.

Tino Pleiner, Masami Hazu, Giovani Pinton Tomaleri, Kurt Januszyk, Robert S Oania, Michael J Sweredoski, Annie Moradian, Alina Guna, Rebecca M Voorhees

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Piezo1 dictates KProceedings of the National Academy of Sciences of the United States of America · 2026
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  10. Structure of the lens MP20 mediated adhesive junction.bioRxiv : the preprint server for biology · 2024
    Article
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  16. WNK1 controls endosomal trafficking through TRIM27-dependent regulation of actin assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

9 authors at 1 institution in 1 country.

Tino PleinerDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Masami HazuDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Giovani Pinton TomaleriDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Kurt JanuszykDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Robert S OaniaDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Michael J SweredoskiDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Annie MoradianDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Alina GunaDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Rebecca M VoorheesDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA. Electronic address: voorhees@caltech.edu.
California Institute of Technology · US

Funding

Protein complex assembly in the ER membraneDP2GM137412 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI VOORHEES, REBECCA · 2019 to 2019
$2.5M
NIGMS NIH HHS DP2 GM137412
6 · The paper itself

Abstract

The assembly of nascent proteins into multi-subunit complexes is a tightly regulated process that must occur at high fidelity to maintain cellular homeostasis. The ER membrane protein complex (EMC) is an essential insertase that requires seven membrane-spanning and two soluble cytosolic subunits to function. Here, we show that the kinase with no lysine 1 (WNK1), known for its role in hypertension and neuropathy, functions as an assembly factor for the human EMC. WNK1 uses a conserved amphipathic helix to stabilize the soluble subunit, EMC2, by binding to the EMC2-8 interface. Shielding this hydrophobic surface prevents promiscuous interactions of unassembled EMC2 and directly competes for binding of E3 ubiquitin ligases, permitting assembly. Depletion of WNK1 thus destabilizes both the EMC and its membrane protein clients. This work describes an unexpected role for WNK1 in protein biogenesis and defines the general requirements of an assembly factor that will apply across the proteome.

Indexed as

Endoplasmic ReticulumHeLa CellsHumansIntracellular MembranesMultiprotein ComplexesWNK Lysine-Deficient Protein Kinase 1Multiprotein ComplexesWNK1 protein, humanWNK Lysine-Deficient Protein Kinase 1amphipathic helixassembly factorhydrophobic interfacekinasemembrane proteinprotein biogenesisprotein complex assemblyprotein quality controlubiquitination

Identifiers

PMID33964204
PMCPMC8254792
OpenAlexW3160370781

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.