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.
Authors	Gina Shaw-Hallgren, Katarzyna Chmielarska Masoumi, Reihaneh Zarrizi, Ulf Hellman, Per Karlsson, Khalil Helou, Ramin Massoumi
Journal	PloS one (PLoS One) Vol. 9 Issue 5 Pg. e96506 ( 2014) ISSN: 1932-6203 [Electronic] United States
PMID	24816797 (Publication Type: Journal Article)
Chemical References	Antineoplastic Agents, Phytogenic HSP27 Heat-Shock Proteins HSPB1 protein, human Heat-Shock Proteins Intracellular Signaling Peptides and Proteins Molecular Chaperones Tumor Necrosis Factor-alpha Etoposide NLK protein, human Protein Serine-Threonine Kinases
Topics	Antineoplastic Agents, Phytogenic (pharmacology) Apoptosis (drug effects, genetics, physiology) Blotting, Western Breast Neoplasms (genetics, metabolism, pathology) Cell Line Cell Line, Tumor Cell Nucleus (metabolism) Cytoplasm (metabolism) Down-Regulation Etoposide (pharmacology) Female HSP27 Heat-Shock Proteins (genetics, metabolism) Heat-Shock Proteins Humans Immunohistochemistry Intracellular Signaling Peptides and Proteins (genetics, metabolism) MCF-7 Cells Microscopy, Confocal Molecular Chaperones Mutation Phosphorylation Protein Binding Protein Serine-Threonine Kinases (genetics, metabolism) RNA Interference Tumor Necrosis Factor-alpha (pharmacology)

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