A central role for the ring finger protein RNF11 in ubiquitin-mediated proteolysis via interactions with E2s and E3s.
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-beta 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.
Connor
Michael K
MK
Molecular and Cellular Biology Research, Laboratory of Molecular Pathology, Rm E-423b, Sunnybrook & Women's College Health Sciences Centre, Toronto, Ontario, Canada.
Seth
Arun
A
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins; D006801:Humans; D008025:Ligases / Q000378:metabolism*; D008954:Models, Biological; D011506:Proteins / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism*
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D011506:Proteins; C404508:RNF11 protein, human; D014452:Ubiquitins; D008025:Ligases