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Is ADRM1 a Good Target for Cancer Therapy?

Is ADRM1 a Good Target for Cancer Therapy? Adhesion-regulating molecule 1 (ADRM1) is a polyubiquitin receptor on the 26th proteasome. It captures substrates by covalently recognizing their ubiquitin chain, and then recruits and activates UCH37 which hydrolyses the ubiquitinated substrates. ADRM1 has been found to be upregulated in many cancers: ovarian, breast, prostrate, colon, cervical and liver cancer, multiple myeloma and, now, acute leukemia. The overexpression of ADRM1 has been linked to increased NF-κB activity [1,2]. IκB-α, a protein that binds to NF-κB and inhibits its nuclear translocation, is one of the substrates of the ADRM1/UCH37 complex. The study by Zheng et al. [3 ]in this issue of Acta Haematologica further confirms the mechanism by elegantly demonstrating increased nuclear fraction of p65, one of the NF-κB proteins, in the presence of overexpressed ADRM1. Inhibiting ADRM1 has also been shown to downregulate the growth factor GIPC1 and upregulate the tumor suppressors RECK and p53 [4,5].Constitutive NF-κB activation has been found in a majority of human cancers, both solid tumors and hematological malignancies. It enhances proliferation, angiogenesis and metastasis as well as suppressing apoptosis, and it would be the most ideal target for cancer therapy were it specific to cancer cells. However, with NF-κB known to be a ubiquitous http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Haematologica Karger

Is ADRM1 a Good Target for Cancer Therapy?

Shenoy, Niraj
Acta Haematologica , Volume 134 (2): 2 – Jan 1, 2015
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Publisher
Karger
Copyright
© 2015 S. Karger AG, Basel
ISSN
0001-5792
eISSN
1421-9662
DOI
10.1159/000381658
Publisher site
See Article on Publisher Site

Abstract

Adhesion-regulating molecule 1 (ADRM1) is a polyubiquitin receptor on the 26th proteasome. It captures substrates by covalently recognizing their ubiquitin chain, and then recruits and activates UCH37 which hydrolyses the ubiquitinated substrates. ADRM1 has been found to be upregulated in many cancers: ovarian, breast, prostrate, colon, cervical and liver cancer, multiple myeloma and, now, acute leukemia. The overexpression of ADRM1 has been linked to increased NF-κB activity [1,2]. IκB-α, a protein that binds to NF-κB and inhibits its nuclear translocation, is one of the substrates of the ADRM1/UCH37 complex. The study by Zheng et al. [3 ]in this issue of Acta Haematologica further confirms the mechanism by elegantly demonstrating increased nuclear fraction of p65, one of the NF-κB proteins, in the presence of overexpressed ADRM1. Inhibiting ADRM1 has also been shown to downregulate the growth factor GIPC1 and upregulate the tumor suppressors RECK and p53 [4,5].Constitutive NF-κB activation has been found in a majority of human cancers, both solid tumors and hematological malignancies. It enhances proliferation, angiogenesis and metastasis as well as suppressing apoptosis, and it would be the most ideal target for cancer therapy were it specific to cancer cells. However, with NF-κB known to be a ubiquitous

Journal

Acta Haematologica – Karger

Published: Jan 1, 2015

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