A central role for the ring finger protein RNF11 in ubiquitin-mediated proteolysis via interactions with E2s and E3s

doi:doi:10.1038/sj.onc.1207380

Oncogene (2004) 23, 2089–2095. doi:10.1038/sj.onc.1207380

A central role for the ring finger protein RNF11 in ubiquitin-mediated proteolysis via interactions with E2s and E3s

Michael K Connor¹ and Arun Seth^1,2

¹Molecular and Cellular Biology Research, Laboratory of Molecular Pathology, Rm E-423b, Sunnybrook & Women's College Health Sciences Centre, Toronto, Ontario, Canada
²Department of Laboratory Medicine and Pathobiology, the CIHR Group in Matrix Dynamics, University of Toronto, 2075 Bayview Avenue, Toronto, Ontario, Canada M4N 3M5

Correspondence: A Seth, Laboratory of Molecular Pathology, Rm E-423b, Sunnybrook & Women's College Health Sciences Centre, 2075 Bayview Avenue, Toronto, Ontario, Canada M4N 3M5. E-mail: arun.seth@utoronto.ca

Top

Abstract

The identification of novel tumor-associated genes represents an important area of cancer research. To that end, we have discovered a number of genes whose expression is altered in breast tumors. One of these genes has been identified as the ring finger protein 11 (RNF11) and its expression is elevated in breast and prostate cancer. The RNF11 gene encodes a 154 amino-acid protein that contains a ring finger and a PY motif. RNF11 is capable of binding numerous proteins, which encompass a wide variety of cellular pathways and mechanisms. This gives RNF11 a corresponding breadth of functions, including involvement in TGF- and epidermal growth factor receptor (EGFR) signaling. In addition, RNF11 has the potential to mediate the ubiquitination and subsequent proteolysis of many cellular proteins. Thus, it may represent an important target of novel cancer therapies.