p62/Sequestosome-1 Associates with and Sustains the Expression of Retroviral Restriction Factor TRIM5α [PDF]
Journal of Virology, 2010 ABSTRACT TRIM5 proteins mediate a potent block to the cross-species transmission of retroviruses, the most well known being the TRIM5α protein from rhesus macaques, which potently inhibits human immunodeficiency virus type 1 (HIV-1) infection. This restriction occurs at an early stage in the replication cycle and is mediated by the binding of
O'Connor Christopher +6 more
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A quest for clarity in bone erosion: The role of sequestosome 1 in Paget's disease of bone. [PDF]
J Biol Chem, 2018 Alterations in the SQSTM1 gene are a putative cause of Paget's disease of bone, yet results are conflicting about how these mutations impact osteoclasts, the cell type believed to be the main pathological contributor. In this issue of JBC, Zach et al.
Michalski MN, Williams BO.
europepmc +4 more sources
A role for sequestosome 1/p62 in mitochondrial dynamics, import and genome integrity
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013 As a signaling scaffold, p62/sequestosome (p62/SQSTM1) plays important roles in cell signaling and degradation of misfolded proteins. While localization of p62 to mitochondria has been reported, a description of its function once there, remains unclear.
Seibenhener, M. Lamar +5 more
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Accumulation of Ubiquitin and Sequestosome-1 Implicate Protein Damage in Diacetyl-Induced Cytotoxicity. [PDF]
Am J Pathol, 2016 Inhaled diacetyl vapors are associated with flavorings-related lung disease, a potentially fatal airway disease. The reactive α-dicarbonyl group in diacetyl causes protein damage in vitro. Dicarbonyl/l-xylulose reductase (DCXR) metabolizes diacetyl into acetoin, which lacks this α-dicarbonyl group.
Hubbs AF +26 more
europepmc +4 more sources
Bcl-2-dependent upregulation of autophagy by sequestosome 1/p62 in vitro. [PDF]
Acta Pharmacol Sin, 2013 To investigate whether sequestosome 1/p62 (p62), a key cargo adaptor protein involved in both the ubiquitin-proteasome system and the autophagy-lysosome system, could directly regulate autophagy in vitro.HEK 293 cells or HeLa cells were transfected with p62-expressing plasmids or siRNA targeting p62.
Zhou L +9 more
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Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease [PDF]
Human Molecular Genetics, 2002 Paget's disease of bone (PDB) is a common disorder characterized by focal abnormalities of increased and disorganized bone turnover. Genetic factors are important in the pathogenesis of PDB, and in previous studies, we and others identified a locus for familial PDB by genome-wide search on 5q35-qter (PDB3). The gene encoding sequestosome 1 (SQSTM1/p62)
Hocking, Lynne J. +11 more
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p62/SQSTM1/Sequestosome-1 is an N-recognin of the N-end rule pathway which modulates autophagosome biogenesis [PDF]
Nature Communications, 2017 Soluble misfolded proteins that fail to be degraded by the ubiquitin proteasome system (UPS) are redirected to autophagy via specific adaptors, such as p62.
Hyunjoo Cha-Molstad +25 more
doaj +2 more sources
Enhanced Epithelial-to-Mesenchymal Transition Associated with Lysosome Dysfunction in Podocytes: Role of p62/Sequestosome 1 as a Signaling Hub [PDF]
Cellular Physiology and Biochemistry, 2015 Background: Autophagy is of importance in the regulation of cell differentiation and senescence in podocytes. It is possible that derangement of autophagy under different pathological conditions activates or enhances Epithelial-to-Mesenchymal Transition (
Guangbi Li +6 more
doaj +2 more sources
PB1 Domain Interaction of p62/Sequestosome 1 and MEKK3 Regulates NF-κB Activation [PDF]
Journal of Biological Chemistry, 2010 p62/Sequestosome 1 is a scaffold protein involved in the regulation of autophagy, trafficking of proteins to the proteasome, and activation of NF-κB. p62 encodes an N-terminal PB1 domain in addition to the ZZ domain, TRAF6-binding domain, LC3 interaction region, and ubiquitin-associated domain, each critical for the physiological function of p62.
Adam J Kimple, David P Siderovski
exaly +3 more sources