Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.
(2014) In PLoS ONE 9(5).- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4455381
- author
- Hallgren, Gina LU ; Masoumi, Katarzyna LU ; Zarrizi, Reihaneh LU ; Hellman, Ulf ; Karlsson, Per ; Helou, Khalil and Massoumi, Ramin LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 9
- issue
- 5
- article number
- e96506
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- pmid:24816797
- wos:000336838000040
- scopus:84901244666
- pmid:24816797
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0096506
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Translational Cancer Research (013250500), Molecular Tumor Pathology (013017570)
- id
- f19f71e7-d2c9-49ad-8c4a-f1c189504875 (old id 4455381)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24816797?dopt=Abstract
- date added to LUP
- 2016-04-01 12:55:12
- date last changed
- 2022-03-06 02:44:10
@article{f19f71e7-d2c9-49ad-8c4a-f1c189504875, 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.}}, author = {{Hallgren, Gina and Masoumi, Katarzyna and Zarrizi, Reihaneh and Hellman, Ulf and Karlsson, Per and Helou, Khalil and Massoumi, Ramin}}, issn = {{1932-6203}}, language = {{eng}}, number = {{5}}, publisher = {{Public Library of Science (PLoS)}}, series = {{PLoS ONE}}, title = {{Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.}}, url = {{https://lup.lub.lu.se/search/files/3045833/4936668.pdf}}, doi = {{10.1371/journal.pone.0096506}}, volume = {{9}}, year = {{2014}}, }