Macroautophagy modulates cellular response to proteasome inhibitors in cancer therapy

TL;DR: This review focuses on the regulation of autophagy by several kinases with particular emphasis on serine/threonine protein kinases such as mTOR, AMP-activated protein kinase, Akt, mitogen-activatedprotein kinase (ERK, p38 and JNK) and protein Kinase C that are often deregulated in cancer and are important therapeutic targets.

TL;DR: A putative mechanism is proposed that could reconcile a role for autophagy in chemotherapy-induced cancer cell death and dampens treatment efficacy, hence providing a therapeutic target to enhance cancer cell killing.

TL;DR: It is shown for the first time that proteasomes were activated in response to pharmacological inhibition of autophagy as well as disruption of autophile-related genes by RNA interference under nutrient-deficient conditions in cultured human colon cancer cells.

TL;DR: This review focuses on the molecular mechanisms of UPS and autophagy in clearance of intracellular protein aggregates, and the relationship between dysregulation of ubiquitin network and diseases.

TL;DR: Understanding autophagy may ultimately allow scientists and clinicians to harness this process for the purpose of improving human health, and to play a role in cell death.

TL;DR: It is demonstrated that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation and p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.

TL;DR: In this article, the authors showed that the polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy by using a 22-residue sequence of p62 containing an evolutionarily conserved motif.

TL;DR: The current understanding of the roles of C/EBP homologous protein (CHOP) and GADD153 in ER stress-mediated apoptosis and in diseases including diabetes, brain ischemia and neurodegenerative disease are summarized.