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Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells
Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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2014 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 9, no 5, e96506- p.Article in journal (Refereed) Published
Abstract [en]

Nemo-like kinase (NLK), a proline-directed serine/threonine kinase regulated by phosphorylation, can be localized in the cytosol or in the nucleus. Whether the localization of NLK can affect cell survival or cell apoptosis is yet to be disclosed. In the present study we found that NLK was mainly localized in the nuclei of breast cancer cells, in contrast to a cytosolic localization in non-cancerous breast epithelial cells. The nuclear localization of NLK was mediated through direct interaction with Heat shock protein 27 (HSP27) which further protected cancer cells from apoptosis. The present study provides evidence of a novel mechanism by which HSP27 recognizes NLK in the breast cancer cells and prevents NLK-mediated cell apoptosis.

Place, publisher, year, edition, pages
2014. Vol. 9, no 5, e96506- p.
National Category
Cancer and Oncology
Identifiers
URN: urn:nbn:se:uu:diva-224629DOI: 10.1371/journal.pone.0096506ISI: 000336838000040PubMedID: 24816797OAI: oai:DiVA.org:uu-224629DiVA: diva2:717439
Available from: 2014-05-15 Created: 2014-05-15 Last updated: 2017-12-05Bibliographically approved

Open Access in DiVA

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