Sequestosome_1

Sequestosome 1

Sequestosome 1

Protein-coding gene in the species Homo sapiens


Sequestosome-1 is a protein that in humans is encoded by the SQSTM1 gene.[5][6][7] Also known as the ubiquitin-binding protein p62,[8] it is an autophagosome cargo protein that targets other proteins that bind to it for selective autophagy. By interacting with GATA4 and targeting it for degradation, it can inhibit GATA-4 associated senescence and senescence-associated secretory phenotype.[9]

Quick Facts SQSTM1, Available structures ...

Mutations in SQSTM1 are a common cause of Paget's disease of bone.[10]

Interactions

Sequestosome 1 has been shown to interact with:


References

  1. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  2. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. Devergne O, Hummel M, Koeppen H, Le Beau MM, Nathanson EC, Kieff E, Birkenbach M (February 1996). "A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes". J Virol. 70 (2): 1143–53. doi:10.1128/JVI.70.2.1143-1153.1996. PMC 189923. PMID 8551575.
  4. Cassidy LD, Narita M (2015). "GATA get a hold on senescence" (PDF). Science. 349 (6255): 1448–9. Bibcode:2015Sci...349.1448C. doi:10.1126/science.aad2501. PMID 26404812. S2CID 35805331.
  5. Layfield R, Ciani B, Ralston S, Hocking L, Sheppard P, Searle M, Cavey J (2004-10-26). "Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone". Biochemical Society Transactions. 32 (5): 728–730. doi:10.1042/bst0320728. ISSN 0300-5127. PMID 15493999. S2CID 22544044.
  6. Shvets E, Fass E, Scherz-Shouval R, Elazar Z (August 2008). "The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes". J. Cell Sci. 121 (Pt 16): 2685–95. doi:10.1242/jcs.026005. PMID 18653543. S2CID 2782335.
  7. Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Mol. Cell. Biol. 18 (5): 3069–80. doi:10.1128/mcb.18.5.3069. PMC 110686. PMID 9566925.
  8. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  9. Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J (1999). "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation". EMBO J. 18 (11): 3044–53. doi:10.1093/emboj/18.11.3044. PMC 1171386. PMID 10356400.
  10. Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J (March 2001). "The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor". J. Biol. Chem. 276 (11): 7709–12. doi:10.1074/jbc.C000869200. PMID 11244088.
  11. Jadhav T, Geetha T, Jiang J, Wooten MW (2008). "Identification of a consensus site for TRAF6/p62 polyubiquitination". Biochem. Biophys. Res. Commun. 371 (3): 521–4. doi:10.1016/j.bbrc.2008.04.138. PMC 2474794. PMID 18457658.
  12. Wooten MW, Geetha T, Babu JR, Seibenhener ML, Peng J, Cox N, Diaz-Meco MT, Moscat J (March 2008). "Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins". J. Biol. Chem. 283 (11): 6783–9. doi:10.1074/jbc.M709496200. PMID 18174161.
  13. Feng, Lifeng et al. “Tamoxifen activates Nrf2-dependent SQSTM1 transcription to promote endometrial hyperplasia” Theranostics vol. 7,7 1890-1900. 10 Apr. 2017, doi:10.7150/thno.19135

Further reading


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