Disease relevance of RNF11

• The potential functions of RNF11-mediated degradation of AMSH in breast cancer are discussed [1].
• One of these genes has been identified as the ring finger protein 11 (RNF11) and its expression is elevated in breast and prostate cancer [2].
• The human RNF11 gene was mapped on chromosome 1p31-p32 region, where frequent alterations have been observed in T-cell acute lymphoblastic leukemia [3].

High impact information on RNF11

• Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2 [1].
• Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif [1].
• The association of RNF11 with these binding partners suggests that it would be involved in biological processes such as gene transcription, BMP/TGF-beta signaling and ubiquitination-associated events [1].
• This gives RNF11 a corresponding breadth of functions, including involvement in TGF-beta and epidermal growth factor receptor (EGFR) signaling [2].
• The RNF11 mRNA was found to be abundant during the proliferation stage of MC3T3-E1 osteoblast development with a short second peak of expression during the mineralization phase [4].

Biological context of RNF11

• Our laboratory has found that the 154aa RING finger protein 11 (RNF11), has modular domains and motifs including a RING-H2 finger domain, a PY motif, an ubiquitin interacting motif (UIM), a 14-3-3 binding sequence and an AKT phosphorylation site [5].
• Immunohistochemical analyses of RNF11 protein encoded by one of the differentially expressed genes revealed it as highly expressed in osteoblasts of multiple skeletal elements during embryonic bone formation in mice [4].
• We used RT-PCR to generate a full-length 2852 nt mRNA sequence that includes the hypothetical open reading frame (ORF) for human RNF11 [6].

Anatomical context of RNF11

• In contrast, cartilage, undifferentiated mesenchymal tissue and osteocytes did not express detectable amounts of the RNF11 protein [4].

Associations of RNF11 with chemical compounds

• Furthermore, treatment of WM239 cells with LY294002 reduces RNF11/14-3-3 interactions suggesting that RNF11/14-3-3 binding is regulated by AKT [7].

Other interactions of RNF11

• Work done in our laboratory has shown that RNF11 is capable of antagonizing Smurf2-mediated inhibition of TGFbeta signalling [5].
• The purpose of this review is to discuss the role of RNF11 in cell signalling and transcription factor modulation with special attention given to the ubiquitin-proteasomal pathway, TGFbeta pathway and EGFR pathway [5].
• Through its association with Smad4 and other transcription factors, RNF11 may have a role in direct transcriptional regulation [5].

Analytical, diagnostic and therapeutic context of RNF11

• Our GST-pulldown and immunoprecipitation results indicate that RNF11 interacts with the E3 ligase AIP4 when coexpressed with RNF11 in mammalian cells [6].

References