Sequestosome 1

SQSTM1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSQSTM1, A170, OSIL, PDB3, ZIP3, p60, p62, p62B, FTDALS3, Sequestosome 1, NADGP, DMRV
External IDsMGI: 107931 HomoloGene: 31202 GeneCards: SQSTM1
Gene location (Human)
Chr.Chromosome 5 (human)[1]
Band5q35.3Start179,806,398 bp[1]
End179,838,078 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

8878

18412

Ensembl

ENSG00000161011
ENSG00000284099

ENSMUSG00000015837

UniProt

Q13501

Q64337

RefSeq (mRNA)

NM_001142298
NM_001142299
NM_003900

NM_001290769
NM_011018

RefSeq (protein)

NP_001135770
NP_001135771
NP_003891

NP_001277698
NP_035148

Location (UCSC)Chr 5: 179.81 – 179.84 MbChr 11: 50.2 – 50.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

Model organisms

Model organisms have been used in the study of SQSTM1 function. A conditional knockout mouse line, called Sqstm1tm1a(KOMP)Wtsi[15][16] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] Twenty two tests were carried out on homozygous mutant mice and one significant abnormality was observed: females had abnormal complete blood count parameters, including an increased red blood cell distribution width and increased mean platelet volume.[13]

Interactions

Sequestosome 1 has been shown to interact with:

References

  1. 1 2 3 ENSG00000284099 GRCh38: Ensembl release 89: ENSG00000161011, ENSG00000284099 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015837 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Joung I, Strominger JL, Shin J (July 1996). "Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain". Proc Natl Acad Sci U S A. 93 (12): 5991–5. doi:10.1073/pnas.93.12.5991. PMC 39176. PMID 8650207.
  6. ↑ 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. PMC 189923. PMID 8551575.
  7. ↑ "Entrez Gene: SQSTM1 sequestosome 1".
  8. ↑ Online Mendelian Inheritance in Man (OMIM) 601530
  9. ↑ Cassidy LD, Narita M (2015). "GATA get a hold on senescence". Science. 349 (6255): 1448–9. doi:10.1126/science.aad2501. PMID 26404812.
  10. ↑ "Haematology data for Sqstm1". Wellcome Trust Sanger Institute.
  11. ↑ "Salmonella infection data for Sqstm1". Wellcome Trust Sanger Institute.
  12. ↑ "Citrobacter infection data for Sqstm1". Wellcome Trust Sanger Institute.
  13. 1 2 3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  14. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  15. ↑ "International Knockout Mouse Consortium".
  16. ↑ "Mouse Genome Informatics".
  17. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  18. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  19. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  20. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  21. ↑ 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.
  22. ↑ 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.
  23. ↑ 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. doi:10.1038/nature04209. PMID 16189514.
  24. ↑ Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J. "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.
  25. ↑ Sanz L, Diaz-Meco MT, Nakano H, Moscat J (April 2000). "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway". EMBO J. 19 (7): 1576–86. doi:10.1093/emboj/19.7.1576. PMC 310227. PMID 10747026.
  26. ↑ 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.
  27. 1 2 Geetha T, Wooten MW (February 2003). "Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling". J. Biol. Chem. 278 (7): 4730–9. doi:10.1074/jbc.M208468200. PMID 12471037.
  28. 1 2 Jadhav T, Geetha T, Jiang J, Wooten MW. "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.
  29. ↑ 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.

Further reading

  • Geetha T, Wooten MW (2002). "Structure and functional properties of the ubiquitin binding protein p62". FEBS Lett. 512 (1–3): 19–24. doi:10.1016/S0014-5793(02)02286-X. PMID 11852044.
  • Layfield R, Ciani B, Ralston SH, Hocking LJ, Sheppard PW, Searle MS, Cavey JR (2005). "Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone". Biochem. Soc. Trans. 32 (Pt 5): 728–30. doi:10.1042/BST0320728. PMID 15493999.
  • Michou L, Collet C, Laplanche JL, Orcel P, Cornélis F (2006). "Genetics of Paget's disease of bone". Joint Bone Spine. 73 (3): 243–8. doi:10.1016/j.jbspin.2005.05.009. PMID 16574459.
  • Park I, Chung J, Walsh CT, Yun Y, Strominger JL, Shin J (1996). "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region". Proc. Natl. Acad. Sci. U.S.A. 92 (26): 12338–42. doi:10.1073/pnas.92.26.12338. PMC 40352. PMID 8618896.
  • Iyer N, Reagan MS, Wu KJ, Canagarajah B, Friedberg EC (1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein". Biochemistry. 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.
  • Vadlamudi RK, Joung I, Strominger JL, Shin J (1996). "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins". J. Biol. Chem. 271 (34): 20235–7. doi:10.1074/jbc.271.34.20235. PMID 8702753.
  • Marcus SL, Winrow CJ, Capone JP, Rachubinski RA (1996). "A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor". J. Biol. Chem. 271 (44): 27197–200. doi:10.1074/jbc.271.44.27197. PMID 8910285.
  • Jallal B, Mossie K, Vasiloudis G, Knyazev P, Zachwieja J, Clairvoyant F, Schilling J, Ullrich A (1997). "The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase". J. Biol. Chem. 272 (18): 12158–63. doi:10.1074/jbc.272.18.12158. PMID 9115287.
  • Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (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.
  • Vadlamudi RK, Shin J (1998). "Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein". FEBS Lett. 435 (2–3): 138–42. doi:10.1016/S0014-5793(98)01021-7. PMID 9762895.
  • 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.
  • Stumptner C, Heid H, Fuchsbichler A, Hauser H, Mischinger HJ, Zatloukal K, Denk H (1999). "Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent". Am. J. Pathol. 154 (6): 1701–10. doi:10.1016/S0002-9440(10)65426-0. PMC 1866621. PMID 10362795.
  • Sudo T, Maruyama M, Osada H (2000). "p62 functions as a p38 MAP kinase regulator". Biochem. Biophys. Res. Commun. 269 (2): 521–5. doi:10.1006/bbrc.2000.2333. PMID 10708586.
  • Sanz L, Diaz-Meco MT, Nakano H, Moscat J (2000). "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway". EMBO J. 19 (7): 1576–86. doi:10.1093/emboj/19.7.1576. PMC 310227. PMID 10747026.
  • Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J (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.
  • Kuusisto E, Salminen A, Alafuzoff I (2001). "Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies". NeuroReport. 12 (10): 2085–90. doi:10.1097/00001756-200107200-00009. PMID 11447312.
  • Laurin N, Brown JP, Lemainque A, Duchesne A, Huot D, Lacourcière Y, Drapeau G, Verreault J, Raymond V, Morissette J (2001). "Paget disease of bone: mapping of two loci at 5q35-qter and 5q31". Am. J. Hum. Genet. 69 (3): 528–43. doi:10.1086/322975. PMC 1235483. PMID 11473345.
  • Chang S, Kim JH, Shin J (2002). "p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition". FEBS Lett. 510 (1–2): 57–61. doi:10.1016/S0014-5793(01)03224-0. PMID 11755531.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.