scispace - formally typeset
Open AccessJournal ArticleDOI

Phosphoregulation of the autophagy machinery by kinases and phosphatases.

Reads0
Chats0
TLDR
In this paper, the authors summarize the current knowledge on kinases and phosphatases acting on the core autophagy machinery and discuss the relevance of phosphoregulation for the overall process of autophagocytosis.
Abstract
Eukaryotic cells use post-translational modifications to diversify and dynamically coordinate the function and properties of protein networks within various cellular processes. For example, the process of autophagy strongly depends on the balanced action of kinases and phosphatases. Highly conserved from the budding yeast Saccharomyces cerevisiae to humans, autophagy is a tightly regulated self-degradation process that is crucial for survival, stress adaptation, maintenance of cellular and organismal homeostasis, and cell differentiation and development. Many studies have emphasized the importance of kinases and phosphatases in the regulation of autophagy and identified many of the core autophagy proteins as their direct targets. In this review, we summarize the current knowledge on kinases and phosphatases acting on the core autophagy machinery and discuss the relevance of phosphoregulation for the overall process of autophagy.

read more

Citations
More filters
Journal ArticleDOI

ER-phagy: mechanisms, regulation, and diseases connected to the lysosomal clearance of the endoplasmic reticulum

TL;DR: ER-phagy is dysfunctional in specific human diseases and its regulators are subverted by pathogens, highlighting its crucial role for cell and organism life.
Journal ArticleDOI

Molecular regulation of autophagosome formation

TL;DR: The current knowledge about the molecular regulation of autophagosome formation is described, with a particular focus on budding yeast and mammalian cells.
Journal ArticleDOI

Molecular regulation of autophagosome formation

TL;DR: A review of the current knowledge about the molecular regulation of autophagosome formation, with a particular focus on budding yeast and mammalian cells, can be found in this article , where the authors describe the current state-of-the-art in autophagy.
Journal ArticleDOI

The AMPK pathway in fatty liver disease

TL;DR: A detailed description of each signaling axis of the AMPK pathway, as well as a discussion of its mechanism of action and therapeutic significance, is performed in this review.
Journal ArticleDOI

Post-Translational Modifications of ATG4B in the Regulation of Autophagy

Na Yeon Park, +2 more
- 01 Apr 2022 - 
TL;DR: Recent advances in understanding of the effect of post-translational modification on the regulation, activity, and function of ATG4, the main protease that controls autophagy are reviewed.
References
More filters
Journal ArticleDOI

A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy.

TL;DR: The identification of the novel protein, Atg 101, and the validation of Atg13 and Atg101 as ULK1-interacting proteins, suggests an Atg1 complex is involved in the induction of macroautophagy in mammalian cells.
Journal ArticleDOI

WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy

TL;DR: The data suggest that WIPI proteins share an evolutionary conserved function in autophagy and that autophagic capacity may be compromised in human cancers.
Journal ArticleDOI

Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast

TL;DR: It is concluded that Tor phosphorylates Tap42 and that phosphorylated Tap42 effectively competes with Cdc55/Tpd3 for binding to the phosphatase 2A catalytic subunit, which establishes Tap42 as a target of Tor and add further refinement to the Tor signaling pathway.
Journal ArticleDOI

Atg17 Functions in Cooperation with Atg1 and Atg13 in Yeast Autophagy

TL;DR: Results indicate that Atg17-Atg13 complex formation plays an important role in normal autophagosome formation via binding to and activating the Atg1 kinase.
Journal ArticleDOI

Why nature chose phosphate to modify proteins

TL;DR: In this manner, phosphorylation serves as a switch that allows signal transduction networks to transmit signals in response to extracellular stimuli, thus promoting inducible protein–protein interaction.
Related Papers (5)