Association of nuclear-localized Nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24816797.
- Also identified by DOI 10.1371/journal.pone.0096506 and PMC identifier 4015990.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Apoptosis
- Breast Neoplasms
- Cell Nucleus
- HSP27 Heat-Shock Proteins
- Intracellular Signaling Peptides and Proteins
- Protein Serine-Threonine Kinases