Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.

Gina Hallgren; Katarzyna Masoumi; Reihaneh Zarrizi; Ulf Hellman; Per Karlsson; Khalil Helou; Ramin Massoumi

doi:10.1371/journal.pone.0096506

Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.

Gina Hallgren, Katarzyna Masoumi, Reihaneh Zarrizi, Ulf Hellman, Per Karlsson, Khalil Helou, Ramin Massoumi

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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.

Original language	English
Article number	e96506
Journal	PLoS ONE
Volume	9
Issue number	5
DOIs	https://doi.org/10.1371/journal.pone.0096506
Publication status	Published - 2014

Bibliographical note

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)

Subject classification (UKÄ)

Cancer and Oncology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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http://www.ncbi.nlm.nih.gov/pubmed/24816797?dopt=Abstract

Cite this

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title = "Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.",

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.",

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note = "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)",

year = "2014",

doi = "10.1371/journal.pone.0096506",

language = "English",

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T1 - Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.

AU - Hallgren, Gina

AU - Masoumi, Katarzyna

AU - Zarrizi, Reihaneh

AU - Hellman, Ulf

AU - Karlsson, Per

AU - Helou, Khalil

AU - Massoumi, Ramin

N1 - 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)

PY - 2014

Y1 - 2014

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AB - 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.

U2 - 10.1371/journal.pone.0096506

DO - 10.1371/journal.pone.0096506

M3 - Article

C2 - 24816797

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JO - PLoS ONE

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ER -

Association of nuclear-localized nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.

Abstract

Bibliographical note

Subject classification (UKÄ)

UN SDGs

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