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Cited by 21Heat shock proteins researchCell death mechanisms and regulationCancer-related Molecular Pathways

Association of Nuclear-Localized Nemo-Like Kinase with Heat-Shock Protein 27 Inhibits Apoptosis in Human Breast Cancer Cells

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Shaw-Hallgren, Gina, Chmielarska Masoumi, Katarzyna, Zarrizi, Reihaneh, Hellman, Ulf, Karlsson, Per, Helou, Khalil, Massoumi, Ramin·2014·PLoS ONE
DOI 10.1371/journal.pone.0096506PMC PMC4015990
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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.

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Crossref · 10.1371/journal.pone.0096506

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  • In breast cancer, NLK is mainly localised in the nuclei of breast cancer cells compared to the cytosolic localisation in non-cancerous breast epithelial cells.

    “In breast cancer, NLK was found to be mainly localised in the nuclei of breast cancer cells compared to the cytosolic localisation in non-cancerous breast epithelial cells.”

    From Nemo-Like Kinase in Development and Diseases: Insights from Mouse Studies (2020) · cites this paper as [29]

  • The interaction between HSP27 and NLK mediates nuclear localisation and protects cancer cells from apoptosis.

    “The interaction between heat shock protein 27 (HSP27) and NLK mediated the nuclear localisation and protected the cancer cells from apoptosis [29].”

    From Nemo-Like Kinase in Development and Diseases: Insights from Mouse Studies (2020) · cites this paper as [29]

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Research works printed but not linked: 39

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Authors
Shaw-Hallgren, G., Chmielarska Masoumi, K., Zarrizi, R., Hellman, U., Karlsson, P., Helou, K., & Massoumi, R.
Affiliations
  • Lund University (SE)
  • Ludwig Cancer Research (SE)
  • University of Gothenburg (SE)
Corresponding author
Massoumi, Ramin
ORCID
Venue
PLoS ONE
Publisher
Public Library of Science (PLoS)
Published
2014-05-09
Volume
9
Issue
5
Pages
e96506
ISSN
1932-6203 (ISSN-L)
DOI
10.1371/journal.pone.0096506
PMC
PMC4015990
OpenAlex
W2032845032
Cited by
21
References
4
Citations by year
2024: 1 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2016: 5 · 2015: 3 · 2014: 1
FWCI
1.23
Type
journal article
Language
en
Open access
Licence
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Uppsala University Publications (Uppsala University) (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • Lund University Publications (Lund University) (submittedVersion, other-oa)
Funders
  • Swedish Cancer Foundation
  • European Commission
  • Kungliga Fysiografiska Sällskapet i Lund
  • Magnus Bergvalls Stiftelse
  • Medical Research Council
  • FP7 Ideas: European Research Council (260460)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords
Nemo-like kinase, HSP27, nuclear localization, apoptosis, breast cancer, cytosolic kinase, cell survival
MeSH terms
Antineoplastic Agents, Phytogenic, Breast Neoplasms, Cell Line, Cell Nucleus, Cytoplasm, Etoposide, Female, Heat-Shock Proteins, Humans, Immunohistochemistry, Mutation, Phosphorylation, Protein Binding, Tumor Necrosis Factor-alpha, Blotting, Western, Down-Regulation, Apoptosis, Protein Serine-Threonine Kinases, Microscopy, Confocal, Molecular Chaperones, RNA Interference, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, HSP27 Heat-Shock Proteins, MCF-7 Cells

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