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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

21 Citeringar (SciVal)
138 Nedladdningar (Pure)

Sammanfattning

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.
Originalspråkengelska
Artikelnummere96506
TidskriftPLoS ONE
Volym9
Utgåva5
DOI
StatusPublished - 2014

Bibliografisk information

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)

Ämnesklassifikation (UKÄ)

  • Cancer och onkologi

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