Evidence map›Paper›PMID 41958020›Full record

ArticleBiophysical journal2026

The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.

Jeriann R Beiter, Dovydas Vasiliauskas, Gillian M Hodge, Hannah E Schneiderman, Monica C Pillon, Sahithya Sridharan Iyer, Michelle C Mendoza, Andrew T Lombardo, Gregory A Voth

Abstract read
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In one paragraph

Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jeriann R BeiterDepartment of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois.
Dovydas VasiliauskasDepartment of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois.
Gillian M HodgeDepartment of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, New York.
Hannah E SchneidermanDepartment of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, New York.
Monica C PillonDepartment of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, New York.
Sahithya Sridharan IyerDepartment of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois.
Michelle C MendozaDepartment of Oncological Sciences, University of Utah, Salt Lake City, Utah; Huntsman Cancer Institute, Salt Lake City, Utah.
Andrew T LombardoDepartment of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, New York. Electronic address: atlombar@buffalo.edu.
Gregory A VothDepartment of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois. Electronic address: gavoth@uchicago.edu.

Funding

New Mechanisms of the Pseudouridine Synthase Module in Mitoribosome AssemblyR35GM147123 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI Monica Pillon · 2022 to 2026
$2.0M
Multiscale Simulation of Key Biomolecular Processes in the CellR35GM158238 · NIGMS · UNIVERSITY OF CHICAGO · PI VOTH, GREGORY A. · 2025 to 2025
$2.0M
Kinase Control of Synergistic Cell Migration MechanicsR01GM141372 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Michelle Christine Mendoza · 2022 to 2026
$1.6M
The Cytoskeletal Drivers of Cell PolarityR35GM156870 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI Andrew Thomas Lombardo · 2025 to 2026
$757k
NIGMS NIH HHS R01 GM141372NIGMS NIH HHS R35 GM147123NIGMS NIH HHS R35 GM156870NIGMS NIH HHS R35 GM158238
6 · The paper itself

Abstract

The lymphocyte-oriented kinase (LOK, also known as STK10) is a critical regulator of membrane tension and an important oncogenic target that mediates the epithelial-to-mesenchymal transition. LOK regulates membrane dynamics through phosphorylation of ezrin/radixin/moesin domain proteins, but the molecular mechanisms through which LOK is able to target to its substrate are yet unknown. Here, we show that LOK and ezrin colocalize at the apical surface of epithelial cells via the LOK C-terminal domain (LOK-CTD). We demonstrate that the LOK-CTD mediates the formation of LOK dimers as well as binding to negatively charged phospholipids and shares structural similarities to inverse Bin/amphiphysin/Rvs domains via a combination of biochemical assays and predictive bioinformatics. We confirm the stability of the LOK-CTD inverse Bin/amphiphysin/Rvs-like dimer via atomistic and coarse-grained molecular dynamics simulations and human cell-based assays to demonstrate the functional significance of the LOK-CTD in mediating colocalization with the FERM domain of ezrin.

Indexed as

Cell MembraneCytoskeletal ProteinsProtein Serine-Threonine KinasesAmino Acid SequenceAnimalsEzrinHumansMolecular Dynamics SimulationProtein BindingProtein DomainsProtein MultimerizationCytoskeletal ProteinsEzrinProtein Serine-Threonine Kinases

Identifiers

PMID41958020
PMCPMC13137150

What OpenQuestion holds

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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.