The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin (Q39731986)

14 September 2017

The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin (English)

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14 September 2017

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Ying-Tsen Tung

1

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14 September 2017

Wen-Ming Hsu

2

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14 September 2017

Hsinyu Lee

3

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14 September 2017

Wei-Pang Huang

4

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14 September 2017

Yung-Feng Liao

5

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14 September 2017

5 March 2010

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Cellular and Molecular Neurobiology

14 September 2017

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14 September 2017

30

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14 September 2017

5

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14 September 2017

795-806

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https://scigraph.springernature.com/pub.10.1007/s10571-010-9507-y

14 September 2017

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Mutation at the cargo-receptor binding site of Atg8 also affects its general autophagy regulation function

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p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

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Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions

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The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8.

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Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion

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A picky eater: exploring the mechanisms of selective autophagy in human pathologies

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Major histocompatibility complex class II-restricted presentation of a cytosolic antigen by autophagy

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Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression

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Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation

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Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes

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cAMP-response element-binding protein contributes to suppression of the A2A adenosine receptor promoter by mutant Huntingtin with expanded polyglutamine residues

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Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch

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Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

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The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes

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12 December 2020

Structural basis for sorting mechanism of p62 in selective autophagy

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12 December 2020

10.1007/S10571-010-9507-Y

Identifiers

DOI

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14 September 2017

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