The inducible E3 ubiquitin ligases SIAH1 and SIAH2 perform critical roles in breast and prostate cancers

Shirley K Knauer; Nisintha Mahendrarajah; Wynand P Roos; Oliver H Krämer

doi:10.1016/j.cytogfr.2015.04.002

The inducible E3 ubiquitin ligases SIAH1 and SIAH2 perform critical roles in breast and prostate cancers

Cytokine Growth Factor Rev. 2015 Aug;26(4):405-13. doi: 10.1016/j.cytogfr.2015.04.002. Epub 2015 May 12.

Authors

Shirley K Knauer¹, Nisintha Mahendrarajah², Wynand P Roos², Oliver H Krämer³

Affiliations

¹ Department of Molecular Biology, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Universitätsstr. 5, 45141 Essen, Germany.
² Department of Toxicology, University Medical Center, Obere Zahlbacher Str. 67, 55131 Mainz, Germany.
³ Department of Toxicology, University Medical Center, Obere Zahlbacher Str. 67, 55131 Mainz, Germany. Electronic address: okraemer@uni-mainz.de.

PMID: 26028498
DOI: 10.1016/j.cytogfr.2015.04.002

Abstract

The ubiquitin-dependent proteasomal degradation of proteins controls signaling and cellular survival. An increasing body of evidence suggests that the E3 ubiquitin ligases SIAH1 and SIAH2 are able to dictate the growth, development, and chemo-/radiosensitivity of breast and prostate cancer cells. Here we review the current knowledge on the impact of SIAHs on breast and prostate tumorigenesis. Furthermore, we summarize how stress, hormones, and cytokines regulate SIAH1 and SIAH2 in transformed mammalian cells.

Keywords: Cytokine; Estrogen; SIAH1; SIAH2; Sex hormone.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Animals
Breast Neoplasms / enzymology*
Breast Neoplasms / genetics
Breast Neoplasms / pathology
Cell Transformation, Neoplastic / metabolism
Cell Transformation, Neoplastic / pathology
Female
Humans
Male
Nuclear Proteins / biosynthesis
Nuclear Proteins / genetics
Nuclear Proteins / metabolism*
Prostatic Neoplasms / enzymology*
Prostatic Neoplasms / genetics
Prostatic Neoplasms / pathology
Ubiquitin-Protein Ligases / biosynthesis
Ubiquitin-Protein Ligases / genetics
Ubiquitin-Protein Ligases / metabolism*

Substances

Nuclear Proteins
Ubiquitin-Protein Ligases
seven in absentia proteins