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Gene Review

RNF11  -  ring finger protein 11

Homo sapiens

Synonyms: CGI-123, MGC51169, RING finger protein 11, SID1669, Sid1669p
 
 
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Disease relevance of RNF11

 

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

References

  1. An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. Li, H., Seth, A. Oncogene (2004) [Pubmed]
  2. A central role for the ring finger protein RNF11 in ubiquitin-mediated proteolysis via interactions with E2s and E3s. Connor, M.K., Seth, A. Oncogene (2004) [Pubmed]
  3. Cloning and expression profile of mouse and human genes, Rnf11/RNF11, encoding a novel RING-H2 finger protein. Seki, N., Hattori, A., Hayashi, A., Kozuma, S., Sasaki, M., Suzuki, Y., Sugano, S., Muramatsu, M.A., Saito, T. Biochim. Biophys. Acta (1999) [Pubmed]
  4. The RING finger protein RNF11 is expressed in bone cells during osteogenesis and is regulated by Ets1. Gao, Y., Ganss, B.W., Wang, H., Kitching, R.E., Seth, A. Exp. Cell Res. (2005) [Pubmed]
  5. RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation. Azmi, P., Seth, A. Eur. J. Cancer (2005) [Pubmed]
  6. The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases. Kitching, R., Wong, M.J., Koehler, D., Burger, A.M., Landberg, G., Gish, G., Seth, A. Biochim. Biophys. Acta (2003) [Pubmed]
  7. Molecular characterization of ring finger protein 11. Connor, M.K., Azmi, P.B., Subramaniam, V., Li, H., Seth, A. Mol. Cancer Res. (2005) [Pubmed]
 
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