ArticleProceedings of the National Academy of Sciences of the United States of America2009
LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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88 citing papers in PubMed, 152 citations in OpenAlex.
- The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.Biophysical journal · 2026Article
- TBXA2R activates ERMs to drive motility, invasion, and metastatic colonization of TNBC cells.Life science alliance · 2026Article
- ERM Inhibition Confers Ferroptosis Resistance through ROS-Induced NRF2 Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Illuminating the Co-Phosphoregulatory Network of the Dark Kinase STK10 by Omics Approaches.BioMed research international · 2026Article
- STK10 emerges from the platelet kinome shadow.Blood · 2026Article
- Mechanism of ERK-mediated Rho Activation and Stress Fiber Assembly for Cell Migration.bioRxiv : the preprint server for biology · 2025Article
- The Immunodeficiency Profile of Lymphocytes in the Patient with Moesin Gene Mutation During Different Infection.Journal of clinical immunology · 2025Article
- OSBPL2 deficiency inhibits Rho/ROCK2/p-ERM signaling and impairs actin cytoskeletal regulation in auditory cells.Journal of biomedical research · 2025Article
- Study of Podoplanin-Deficient Mouse Bone with Mechanical Stress.Dentistry journal · 2025Article
- RNAi library screening reveals Gβ1, Casein Kinase 2 and ICAP-1 as novel regulators of LFA-1-mediated T cell polarity and migration.Immunology and cell biology · 2025Article
- TNIK: A redox sensor in endothelial cell permeability.Science advances · 2024Article
- Organization of a cytoskeletal superstructure in the apical domain of intestinal tuft cells.The Journal of cell biology · 2024Article
- Ezrin drives adaptation of monocytes to the inflamed lung microenvironment.Cell death & disease · 2024Article
- Radixin: Roles in the Nervous System and Beyond.Biomedicines · 2024Review
- CRABP1-complexes in exosome secretion.Cell communication and signaling : CCS · 2024Article
- Article
- ELM-the Eukaryotic Linear Motif resource-2024 update.Nucleic acids research · 2024Article
- Stk10 Deficiency in Mice Promotes Tumor Growth by Dysregulating the Tumor Microenvironment.Biology · 2022Article
- Bidirectional feedback between BCR signaling and actin cytoskeletal dynamics.The FEBS journal · 2022Review
- A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.Biophysical reviews · 2022Review
28 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
ERM (ezrin-radixin-moesin) proteins mediate linkage of actin cytoskeleton to plasma membrane in many cells. ERM activity is regulated in part by phosphorylation at a C-terminal threonine, but the identity of ERM kinases is unknown in lymphocytes and incompletely defined in other mammalian cells. Our studies show that lymphocyte-oriented kinase (LOK) is an ERM kinase in vitro and in vivo. Mass spectrometric analysis indicates LOK is abundant at the lymphocyte plasma membrane and immunofluorescence studies show LOK enrichment at the plasma membrane near ERM. In vitro peptide specificity analyses characterize LOK as a basophilic kinase whose optimal substrate sequence resembles the ERM site, including unusual preference for tyrosine at P-2. LOK's activity on moesin peptide and protein was comparable to reported ERM kinases ROCK and PKC but unlike them LOK displayed preferential specificity for moesin compared to traditional basophilic kinase substrates. Two genetic approaches demonstrate a role for LOK in ERM phosphorylation: cell transfection with LOK kinase domain augments ERM phosphorylation and lymphocytes from LOK knockout mice have >50% reduction in ERM phosphorylation. The findings on localization and specificity argue that LOK is a direct ERM kinase. The knockout mice have normal hematopoietic cell development but notably lymphocyte migration and polarization in response to chemokine are enhanced. These functional alterations fit the current understanding of the role of ERM phosphorylation in regulating cortical reorganization. Thus, these studies identify a new ERM kinase of importance in lymphocytes and confirm the role of ERM phosphorylation in regulating cell shape and motility.
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