scholarly journals ATG8ylation of proteins: A way to cope with cell stress?

2021 ◽  
Vol 220 (11) ◽  
Author(s):  
Julian M. Carosi ◽  
Thanh N. Nguyen ◽  
Michael Lazarou ◽  
Sharad Kumar ◽  
Timothy J. Sargeant

The ATG8 family of proteins regulates autophagy in a variety of ways. Recently, ATG8s were demonstrated to conjugate directly to cellular proteins in a process termed “ATG8ylation,” which is amplified by mitochondrial damage and antagonized by ATG4 proteases. ATG8s may have an emerging role as small protein modifiers.

2018 ◽  
Vol 122 (5) ◽  
pp. 489-500 ◽  
Author(s):  
Tomás Lombardo ◽  
Martín Gil Folgar ◽  
Luciana Salaverry ◽  
Estela Rey-Roldán ◽  
Elida M. Alvarez ◽  
...  

2021 ◽  
Author(s):  
Odetta Antico ◽  
Erica Barini ◽  
Miratul M. K. Muqit

Upon mitochondrial damage, activation of the PINK1 kinase and Parkin ubiquitin ligase induces ubiquitylation of multiple proteins at the mitochondria to stimulate their elimination by mitophagy. Protein ubiquitylation is a highly dynamic, reversible and complex post-translation modification (PTM) and it is frequently linked with phosphorylation. The major challenges, for biochemical and quantitative proteomic analysis of cellular proteins that are ubiquitylated and phosphorylated in response to mitochondrial damage in a PINK1-Parkin-dependent manner, involve the spatial configuration and stoichiometry of these post-translational modifications occurring on the mitochondria. Here, we describe an optimised protocol to isolate membrane-enriched fractions that provides high mitochondrial yield from primary cells, such as neuronal cultures. This protocol, in combination with other enrichment strategies, will facilitate proteomic and biochemical workflows for investigation of molecular events defined by PINK1/Parkin pathway.


2009 ◽  
Vol 47 (05) ◽  
Author(s):  
J Maléth ◽  
Z Rakonczay ◽  
V Venglovecz ◽  
Z Rázga ◽  
L Tiszlavicz ◽  
...  

Author(s):  
Martin Reynders ◽  
Bryan Matsuura ◽  
Marleen Bérouti ◽  
Daniele Simoneschi ◽  
Antonio Marzio ◽  
...  

<p><i>PROTACs (proteolysis targeting chimeras) are bifunctional molecules that tag proteins for ubiquitylation by an E3 ligase complex and subsequent degradation by the proteasome. They have emerged as powerful tools to control the levels of specific cellular proteins and are on the verge of being clinically used. We now introduce photoswitchable PROTACs that can be activated with the temporal and spatial precision that light provides. These trifunctional molecules, which we named PHOTACs, consist of a ligand for an E3 ligase, a photoswitch, and a ligand for a protein of interest. We demonstrate this concept by using PHOTACs that target either BET family proteins (BRD2,3,4) or FKBP12. Our lead compounds display little or no activity in the dark but can be reversibly activated to varying degrees with different wavelengths of light. Our modular and generalizable approach provides a method for the optical control of protein levels with photopharmacology and could lead to new types of precision therapeutics that avoid undesired systemic toxicity.</i><b></b></p>


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