Brinda Ravikumar

TL;DR: This work shows that mammalian target of rapamycin (mTOR) is sequestered in polyglutamine aggregates in cell models, transgenic mice and human brains, and provides proof-of-principle for the potential of inducing autophagy to treat Huntington disease.

TL;DR: This review focuses on mammalian autophagy, and an overview of the understanding of its machinery and the signaling cascades that regulate it is given, and the possibility of autophagic upregulation as a therapeutic approach for various conditions is considered.

TL;DR: It was found that not only is α-synuclein degraded by the proteasome, but it is also degraded by autophagy, which merits consideration as a potential therapeutic for Parkinsons disease, as it is designed for chronic use in humans.

TL;DR: Exon 1 of the HD gene with expanded polyglutamine [poly(Q)] repeats and enhanced green fluorescent protein tagged to 19 alanines is used as models for aggregate-prone proteins, to investigate the pathways mediating their degradation and re-examined the role of the proteasome.

TL;DR: It is shown in mammalian cells that the heavy chain of clathrin interacts with Atg16L1 and is involved in the formation of Atg 16L1-positive early autophagosome precursors, and the plasma membrane contributes directly to the formation.