Journal ArticleDOI
Autophagy Receptors and Neurodegenerative Diseases.
Zhiqiang Deng,Zhiqiang Deng,Zhiqiang Deng,Kerry Purtell,Véronik Lachance,Mitchell S. Wold,Shi Chen,Shi Chen,Zhenyu Yue +8 more
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TLDR
Recent advances in understanding the physiology and pathophysiology of autophagy receptors in selective autophapy are reviewed, and their potentials as therapeutic targets for neurodegenerative diseases are discussed.About:
This article is published in Trends in Cell Biology.The article was published on 2017-07-01. It has received 160 citations till now. The article focuses on the topics: Autophagy database & Autophagy.read more
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The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
TL;DR: The complexity of the ubiquitin code is overviewed, with an emphasis on the emerging role of linkage-specific degradation signals (degrons) in the Ubiquitin-proteasome system (UPS) and the autophagy-lysosome system
Journal ArticleDOI
Regulation of selective autophagy: the p62/SQSTM1 paradigm
TL;DR: Autophagy receptors can induce local recruitment and activation of ULK1/2 and PI3KC3 complexes at the site of cargo sequestration, and Regulation of the capacity of the core autophagy machinery also affects selective autophagic.
Journal ArticleDOI
Intrinsically Disordered Protein TEX264 Mediates ER-phagy.
TL;DR: A differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy).
Journal ArticleDOI
Crosstalk and Interplay between the Ubiquitin-Proteasome System and Autophagy.
Chang Hoon Ji,Yong Tae Kwon +1 more
TL;DR: The mechanisms underlying the crosstalk and interplay between the UPS and autophagy are discussed, with an emphasis on substrate selectivity and compensatory regulation under cellular stresses.
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ATL3 Is a Tubular ER-Phagy Receptor for GABARAP-Mediated Selective Autophagy.
TL;DR: It is shown that ATL3 functions as a receptor for ER-phagy, promoting tubular ER degradation upon starvation, and a new ATL3 function for GABARAP-mediated ER- phagy in the degradation of tubularER is revealed.
References
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Journal ArticleDOI
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
Marcy E. MacDonald,Christine Ambrose,Mabel P. Duyao,Richard H. Myers,Carol Lin,Lakshmi Srinidhi,Glenn Barnes,Sherryl A.M. Taylor,Marianne James,Nicolet Groot,Heather MacFarlane,Barbara Jenkins,Mary Anne Anderson,Nancy S. Wexler,James F. Gusella,Gillian P. Bates,Sarah Baxendale,Holger Hummerich,Susan F. Kirby,Mike North,S. Youngman,Richard Mott,Günther Zehetner,Zdenek Sedlacek,Annemarie Poustka,Anna-Maria Frischauf,Hans Lehrach,Alan Buckler,Deanna M. Church,Lynn Doucette-Stamm,Michael Conlon O'Donovan,Laura Riba-Ramirez,Manish A. Shah,Vincent P. Stanton,Scott A. Strobel,Karen M. Draths,Jennifer L. Wales,Peter B. Dervan,David E. Housman,Michael R. Altherr,Rita Shiang,Leslie M. Thompson,Thomas J. Fielder,John J. Wasmuth,Danilo A. Tagle,John Valdes,Lawrence W. Elmer,Marc W. Allard,Lucio H. Castilla,Manju Swaroop,Kris Blanchard,Francis S. Collins,Russell G. Snell,Tracey Holloway,Kathleen Gillespie,Nicole A. Datson,Duncan Shaw,Peter S. Harper +57 more
TL;DR: In this article, the authors used haplotype analysis of linkage disequilibrium to spotlight a small segment of 4p16.3 as the likely location of the defect, which is expanded and unstable on HD chromosomes.
Journal Article
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group.
Manish A. Shah,Nicole A. Datson,Lakshmi Srinidhi,Vincent P. Stanton,Marcy E. MacDonald,Marc W. Allard,S. Youngman,Anna-Maria Frischauf,Richard Mott,KM Draths,Günther Zehetner,C. O’Donovan,Thomas J. Fielder,Bruce G. Jenkins,Manju Swaroop,Sherryl A.M. Taylor,Lynn Doucette-Stamm,Heather MacFarlane,Scott A. Strobel,H. E. McFarlane,Alan Buckler,Nicolet Groot,Holger Hummerich,Deanna M. Church,M. A. Anderson,Marianne James,Glenn Barnes,M. Christine,Francis S. Collins,Mabel P. Duyao,Peter B. Dervan,Gillian P. Bates,T Holloway,Peter S. Harper,TW Mcdonald,M North,K Blanchard,John J. Wasmuth,D. Shaw,Hans Lehrach,Danilo A. Tagle,Annemarie Poustka,David E. Housman,T. Huntington,Zdenek Sedlacek,Laura Riba,Susan F. Kirby,Carol Lin,Richard H. Myers,Leslie M. Thompson,Russell G. Snell,Michael Conlon O'Donovan,K Gillespie,Rita Shiang,Nancy S. Wexler,Christine Ambrose,J. F. Gusella,Sarah Baxendale,N. Groat,John Valdes +59 more
TL;DR: The Huntington's disease mutation involves an unstable DNA segment, similar to those described in fragile X syndrome, spino-bulbar muscular atrophy, and myotonic dystrophy, acting in the context of a novel 4p16.3 gene to produce a dominant phenotype.
Journal ArticleDOI
Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
Marian DiFiglia,Ellen Sapp,Kathryn Chase,Stephen W. Davies,Gillian P. Bates,J. P. Vonsattel,Neil Aronin +6 more
TL;DR: An NH2-terminal fragment of mutant huntingtin was localized to neuronal intranuclear inclusions and dystrophic neurites in the HD cortex and striatum, and polyglutamine length influenced the extent of huntingtin accumulation in these structures.
Journal ArticleDOI
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
Geir Bjørkøy,Trond Lamark,Andreas Brech,Heidi Outzen,Maria Perander,Aud Øvervatn,Harald Stenmark,Terje Johansen +7 more
TL;DR: In this article, the polyubiquitin-binding protein p62/SQSTM1 has been shown to be involved in linking polyUBiquitinated protein aggregates to the autophagy machinery.
Journal ArticleDOI
The Role of Atg Proteins in Autophagosome Formation
TL;DR: The molecular mechanism of autophagosome formation is described with particular focus on the function of Atg proteins and the long-standing discussion regarding the origin of the autophagous membrane membrane.