Crystal Structure of the Ubiquitin-associated (UBA) Domain of p62 and Its Interaction with Ubiquitin
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Title
Crystal Structure of the Ubiquitin-associated (UBA) Domain of p62 and Its Interaction with Ubiquitin
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 36, Pages 31864-31874
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2011-06-30
DOI
10.1074/jbc.m111.259630
References
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Note: Only part of the references are listed.- Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy
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- C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation
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- PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
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- p62 at the Crossroads of Autophagy, Apoptosis, and Cancer
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- Essential Role of Sequestosome 1/p62 in Regulating Accumulation of Lys63-ubiquitinated Proteins
- (2008) Marie W. Wooten et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Basis for Sorting Mechanism of p62 in Selective Autophagy
- (2008) Yoshinobu Ichimura et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Ref(2)P, theDrosophila melanogasterhomologue of mammalian p62, is required for the formation of protein aggregates in adult brain
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- Midbody ring disposal by autophagy is a post-abscission event of cytokinesis
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- Affinity Makes the Difference: Nonselective Interaction of the UBA Domain of Ubiquilin-1 with Monomeric Ubiquitin and Polyubiquitin Chains
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