ArticleThe Biochemical journal2014
MEKK2 regulates paxillin ubiquitylation and localization in MDA-MB 231 breast cancer cells.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- TRIM15 Mediates ubiquitination of Paxillin to facilitate the progression of ovarian cancer.Cancer cell international · 2026Article
- Paxillin and Kindlin: Research Progress and Biological Functions.Biomolecules · 2025Review
- Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators.International journal of molecular sciences · 2021Review
- Rab40-Cullin5 complex regulates EPLIN and actin cytoskeleton dynamics during cell migration.The Journal of cell biology · 2021Article
- Silencing of the MEKK2/MEKK3 Pathway Protects against Spinal Cord Injury via the Hedgehog Pathway and the JNK Pathway.Molecular therapy. Nucleic acids · 2019Article
- Discovery and characterization of an iminocoumarin scaffold as an inhibitor of MEKK2 (MAP3K2).Biochemical and biophysical research communications · 2018Article
- Oncogenic signaling of MEK5-ERK5.Cancer letters · 2017Review
- Interaction with the Paxillin LD1 Motif Relieves MEKK2 Auto-inhibition.Journal of molecular signaling · 2015Article
- Identification of ponatinib and other known kinase inhibitors with potent MEKK2 inhibitory activity.Biochemical and biophysical research communications · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The intracellular kinase MEKK2 (mitogen-activated protein kinase/extracellular-signal-regulated kinase kinase kinase 2) is an upstream regulator of JNK (c-Jun N-terminal kinase), but additional functions for MEKK2 have not been well defined. Silencing MEKK2 expression in invasive breast tumour cells markedly inhibits xenograft metastasis, indicating that MEKK2 controls tumour cell function required for tumour progression. In our previous investigation of MEKK2 function, we discovered that tumour cell attachment to fibronectin recruits MEKK2 to focal adhesion complexes, and that MEKK2 knockdown is associated with stabilized focal adhesions and significant inhibition of tumour cell migration. In the present study we investigate MEKK2 function in focal adhesions and we report that MEKK2 physically associates with the LD1 motif of the focal adhesion protein paxillin. We reveal that MEKK2 induces paxillin ubiquitylation, and that this function requires both the paxillin LD1 motif and MEKK2 kinase activity. Finally, we demonstrate that MEKK2 promotes paxillin redistribution from focal adhesions into the cytoplasm, but does not promote paxillin degradation. Taken together, our results reveal a novel function for MEKK2 as a regulator of ubiquitylation-dependent paxillin redistribution in breast tumour cells.
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Registered trials
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.