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.
authors.affiliation: Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
authors.forename: Gina
authors.initials: G
authors.lastname: Shaw-Hallgren
authors.affiliation: Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Chmielarska Masoumi
authors.affiliation: Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
authors.forename: Reihaneh
authors.initials: R
authors.lastname: Zarrizi
authors.affiliation: Ludwig Institute for Cancer Research, Uppsala, Sweden.
authors.forename: Ulf
authors.initials: U
authors.lastname: Hellman
authors.affiliation: Institute of Clinical Sciences, Department of Oncology, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Per
authors.initials: P
authors.lastname: Karlsson
authors.affiliation: Institute of Clinical Sciences, Department of Oncology, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Khalil
authors.initials: K
authors.lastname: Helou
authors.affiliation: Translational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
authors.forename: Ramin
authors.initials: R
authors.lastname: Massoumi
mesh_terms: D000972:Antineoplastic Agents, Phytogenic / Q000494:pharmacology; D017209:Apoptosis / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D015153:Blotting, Western; D001943:Breast Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D002460:Cell Line; D045744:Cell Line, Tumor; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D015536:Down-Regulation; D005047:Etoposide / Q000494:pharmacology; D005260:Female; D055551:HSP27 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006360:Heat-Shock Proteins; D006801:Humans; D007150:Immunohistochemistry; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism*; D061986:MCF-7 Cells; D018613:Microscopy, Confocal; D018832:Molecular Chaperones; D009154:Mutation; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology
chemical_list: D000972:Antineoplastic Agents, Phytogenic; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones; D014409:Tumor Necrosis Factor-alpha; D005047:Etoposide; C470551:NLK protein, human; D017346:Protein Serine-Threonine Kinases