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SIPA1L1  -  signal-induced proliferation-associated 1...

Homo sapiens

Synonyms: E6-targeted protein 1, E6TP1, High-risk human papilloma viruses E6 oncoproteins targeted protein 1, KIAA0440, SIPA1-like protein 1, ...
 
 
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Disease relevance of SIPA1L1

 

High impact information on SIPA1L1

  • The mRNA for E6TP1 is widely expressed in tissues and in vitro-cultured cell lines [1].
  • Furthermore, the E6-binding region of E6TP1 complexes with E6AP via E6 [3].
  • We have reported previously that the high-risk human papillomavirus (HPV) E6 oncoprotein interacts with E6TP1, a novel Rap GTPase-activating protein (RapGAP) [3].
  • Similar to p53 tumor suppressor protein, the high-risk HPV E6 oncoproteins target E6TP1 for degradation [3].
  • The HPV16 E6-induced degradation of E6TP1 strongly correlates with its ability to immortalize human mammary epithelial cells [3].
 

Biological context of SIPA1L1

  • Analysis of the roles of E6 binding to E6TP1 and nuclear localization in the human papillomavirus type 31 life cycle [4].
  • Mutation of amino acid 128 in HPV 31 E6 was found to abrogate the ability to bind and degrade E6TP1 but did not alter binding to another alpha-helical domain protein, E6AP [4].
 

Associations of SIPA1L1 with chemical compounds

  • Tuberin and E6TP1 protein levels are tightly regulated through ubiquitin-mediated proteolysis [5].
 

Regulatory relationships of SIPA1L1

  • Importantly, the purified E6AP enhanced the ubiquitination and degradation of E6TP1 in the presence of E6 in vitro [3].
 

Other interactions of SIPA1L1

  • Human papillomavirus E6-induced degradation of E6TP1 is mediated by E6AP ubiquitin ligase [3].
  • Using two different approaches, we now demonstrate that human E6TP1 exhibits GAP activity for Rap1 and Rap2, confirming recent findings that a closely related rat homologue exhibits Rap-specific GAP activity [6].
  • We observed a strict correlation between the ability of E6 protein to target E6TP1 for degradation and its ability to immortalize MECs [7].
  • As a region within E6TP1 has high homology with GAP domains of known and putative Rap GTPase-activating proteins (GAPs), these results raised the possibility that HPV E6 may alter the Rap small-G-protein signaling pathway [6].

References

  1. The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation. Gao, Q., Srinivasan, S., Boyer, S.N., Wazer, D.E., Band, V. Mol. Cell. Biol. (1999) [Pubmed]
  2. Interaction of the human papillomavirus type 16 E6 oncoprotein with wild-type and mutant human p53 proteins. Scheffner, M., Takahashi, T., Huibregtse, J.M., Minna, J.D., Howley, P.M. J. Virol. (1992) [Pubmed]
  3. Human papillomavirus E6-induced degradation of E6TP1 is mediated by E6AP ubiquitin ligase. Gao, Q., Kumar, A., Singh, L., Huibregtse, J.M., Beaudenon, S., Srinivasan, S., Wazer, D.E., Band, H., Band, V. Cancer Res. (2002) [Pubmed]
  4. Analysis of the roles of E6 binding to E6TP1 and nuclear localization in the human papillomavirus type 31 life cycle. Lee, C., Wooldridge, T.R., Laimins, L.A. Virology (2007) [Pubmed]
  5. Thyroid-stimulating hormone/cAMP and glycogen synthase kinase 3beta elicit opposing effects on Rap1GAP stability. Tsygankova, O.M., Feshchenko, E., Klein, P.S., Meinkoth, J.L. J. Biol. Chem. (2004) [Pubmed]
  6. The high-risk human papillomavirus type 16 E6 counters the GAP function of E6TP1 toward small Rap G proteins. Singh, L., Gao, Q., Kumar, A., Gotoh, T., Wazer, D.E., Band, H., Feig, L.A., Band, V. J. Virol. (2003) [Pubmed]
  7. Human papillomavirus type 16 E6-induced degradation of E6TP1 correlates with its ability to immortalize human mammary epithelial cells. Gao, Q., Singh, L., Kumar, A., Srinivasan, S., Wazer, D.E., Band, V. J. Virol. (2001) [Pubmed]
 
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