Sequestosome: Difference between revisions
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<StructureSection load=' | <StructureSection load='2jy8' size='340' side='right' caption='Structure of human sequestosome UBA domain (PDB code [[2jy8]])' scene=''> | ||
== Function == | == Function == | ||
'''Sequestosome''' (SQS) or '''p62''', is required for the formation and autophagic degredation of polyubiquitin-containg bodies. SQS may regulate signaling cascades through ubiquitination<ref>PMID:15340068</ref>. | |||
== Structural highlights == | |||
SQS is a multi-domain protein. SQS domain structure includes: <br /> | SQS is a multi-domain protein. SQS domain structure includes: <br /> | ||
PB1 domain which contains Phox and Berm1<br /> | *PB1 domain which contains Phox and Berm1<br /> | ||
ZZ-type zinc finger <br /> | *ZZ-type zinc finger <br /> | ||
SMIR – SOD interaction domain<br /> | *SMIR – SOD interaction domain<br /> | ||
TB – TRAF6 binding motif<br /> | *TB – TRAF6 binding motif<br /> | ||
LC3 – microtubule-associated protein 1 light chain 3B<br /> | *LC3 – microtubule-associated protein 1 light chain 3B<br /> | ||
LIR – interaction region<br /> | *LIR – interaction region<br /> | ||
UBA – ubiquitin association domain. | *UBA – ubiquitin association domain. | ||
== Relevance == | == Relevance == | ||
SQS is associated with fibrillary tangles in Alzheimer disease<ref>PMID:22138392</ref>. | |||
==3D structures of sequestosome== | ==3D structures of sequestosome== | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
[[1q02]], [[2jy7]], [[2jy8]], [[2k0b]], [[2knv]] – | Domains: PB1 1-102; ZZ 120-180; UBA 387-436 | ||
[[ | |||
[[ | [[1q02]], [[2jy7]], [[2jy8]], [[2k0b]], [[2knv]] – hSQS UBA domain – human - NMR<br /> | ||
[[6jm4]] – hSQS-1 PB1 domain (mutant)<br /> | |||
[[4uf8]], [[4uf9]], [[6tgy]], [[6th3]] – hSQS-1 PB1 domain – Cryo EM<br /> | |||
[[5yp7]], [[5yp8]], [[5ypa]], [[5ypb]], [[5ypc]], [[5ype]], [[5ypg]], [[5yph]], [[5ypi]], [[6miu]] – hSQS-1 ZZ domain<br /> | |||
[[6mj7]] – hSQS-1 ZZ domain + Arg<br /> | |||
[[6khz]] – hSQS-1 ZZ domain + Gly<br /> | |||
[[7r1o]] – hSQS-1 ZZ domain + drug<br /> | |||
[[2ktr]] – rSQS PB1 domain – rat - NMR<br /> | [[2ktr]] – rSQS PB1 domain – rat - NMR<br /> | ||
[[2kkc]] – rSQS PB1 domain (mutant) - NMR<br /> | [[2kkc]] – rSQS PB1 domain (mutant) - NMR<br /> | ||
[[ | [[4mjs]] – hSQS-1 PB1 domain + protein kinase C zeta type<br /> | ||
[[3b0f]] – mSQS UBA domain – mouse <br /> | |||
[[2rru]] – mSQS UBA domain - NMR<br /> | |||
Latest revision as of 11:28, 15 November 2023
FunctionSequestosome (SQS) or p62, is required for the formation and autophagic degredation of polyubiquitin-containg bodies. SQS may regulate signaling cascades through ubiquitination[1]. Structural highlightsSQS is a multi-domain protein. SQS domain structure includes:
RelevanceSQS is associated with fibrillary tangles in Alzheimer disease[2]. 3D structures of sequestosomeUpdated on 17-May-2025 Domains: PB1 1-102; ZZ 120-180; UBA 387-436 1q02, 2jy7, 2jy8, 2k0b, 2knv – hSQS UBA domain – human - NMR 6jm4 – hSQS-1 PB1 domain (mutant)
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ReferencesReferences
- ↑ Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol. 2004 Sep;24(18):8055-68. PMID:15340068 doi:10.1128/MCB.24.18.8055-8068.2004
- ↑ Salminen A, Kaarniranta K, Haapasalo A, Hiltunen M, Soininen H, Alafuzoff I. Emerging role of p62/sequestosome-1 in the pathogenesis of Alzheimer's disease. Prog Neurobiol. 2012 Jan;96(1):87-95. doi: 10.1016/j.pneurobio.2011.11.005. Epub , 2011 Nov 22. PMID:22138392 doi:http://dx.doi.org/10.1016/j.pneurobio.2011.11.005