Nature Communications (Sep 2021)
TNK1 is a ubiquitin-binding and 14-3-3-regulated kinase that can be targeted to block tumor growth
- Tsz-Yin Chan,
- Christina M. Egbert,
- Julia E. Maxson,
- Adam Siddiqui,
- Logan J. Larsen,
- Kristina Kohler,
- Eranga Roshan Balasooriya,
- Katie L. Pennington,
- Tsz-Ming Tsang,
- Madison Frey,
- Erik J. Soderblom,
- Huimin Geng,
- Markus Müschen,
- Tetyana V. Forostyan,
- Savannah Free,
- Gaelle Mercenne,
- Courtney J. Banks,
- Jonard Valdoz,
- Clifford J. Whatcott,
- Jason M. Foulks,
- David J. Bearss,
- Thomas O’Hare,
- David C. S. Huang,
- Kenneth A. Christensen,
- James Moody,
- Steven L. Warner,
- Jeffrey W. Tyner,
- Joshua L. Andersen
Affiliations
- Tsz-Yin Chan
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Christina M. Egbert
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Julia E. Maxson
- Division of Hematology & Medical Oncology, Knight Cancer Institute, Oregon Health & Science University
- Adam Siddiqui
- Sumitomo Dainippon Pharma Oncology
- Logan J. Larsen
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Kristina Kohler
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Eranga Roshan Balasooriya
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Katie L. Pennington
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Tsz-Ming Tsang
- Department of Chemistry and Biochemistry, Brigham Young University
- Madison Frey
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Erik J. Soderblom
- Proteomics and Metabolomics Shared Resource, Duke University School of Medicine
- Huimin Geng
- Department of Laboratory Medicine, University of California San Francisco
- Markus Müschen
- Department of Systems Biology, City of Hope Comprehensive Cancer Center
- Tetyana V. Forostyan
- Sumitomo Dainippon Pharma Oncology
- Savannah Free
- Sumitomo Dainippon Pharma Oncology
- Gaelle Mercenne
- Sumitomo Dainippon Pharma Oncology
- Courtney J. Banks
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Jonard Valdoz
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- Clifford J. Whatcott
- Sumitomo Dainippon Pharma Oncology
- Jason M. Foulks
- Sumitomo Dainippon Pharma Oncology
- David J. Bearss
- Sumitomo Dainippon Pharma Oncology
- Thomas O’Hare
- Division of Hematology and Hematologic Malignancies, Huntsman Cancer Institute, University of Utah
- David C. S. Huang
- The Walter and Eliza Hall Institute of Medical Research
- Kenneth A. Christensen
- Department of Chemistry and Biochemistry, Brigham Young University
- James Moody
- Department of Chemistry and Biochemistry, Brigham Young University
- Steven L. Warner
- Sumitomo Dainippon Pharma Oncology
- Jeffrey W. Tyner
- Division of Hematology & Medical Oncology, Knight Cancer Institute, Oregon Health & Science University
- Joshua L. Andersen
- Fritz B. Burns Cancer Research Laboratory, Brigham Young University
- DOI
- https://doi.org/10.1038/s41467-021-25622-3
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 17
Abstract
The mechanisms underlying the activity of non-receptor tyrosine kinase, TNK1, in cancers are unclear. Here the authors show that MARK mediates 14-3-3 and TNK1 interaction which restrains TNK1 activity, while the release of TNK1 from 14-3-3 leads to TNK1 activation through its interaction with ubiquitin and thus results in TNK1-mediated tumor growth in vivo
