Abstract
Autophagy is an intracellular catabolic system that delivers cytoplasmic constituents and organelles in the vacuole. This degradative process is mediated by a group of proteins coded by autophagy-related (ATG) genes that are widely conserved from yeasts to plants and mammals. Homologs of ATG genes have been also identified in algal genomes including the unicellular model green alga Chlamydomonas reinhardtii. The development of specific tools to monitor autophagy in Chlamydomonas has expanded our current knowledge about the regulation and function of this process in algae. Recent findings indicated that autophagy is regulated by redox signals and the TOR network in Chlamydomonas and revealed that this process may play in important role in the control of lipid metabolism and ribosomal protein turnover in this alga. Here, we will describe the different techniques and approaches that have been reported to study autophagy and autophagic flux in Chlamydomonas.
Highlights
Eukaryotic cells are able to degrade intracellular material through a membrane-trafficking process known as autophagy
Recent findings indicated that autophagy is regulated by redox signals and the TOR network in Chlamydomonas and revealed that this process may play in important role in the control of lipid metabolism and ribosomal protein turnover in this alga
The unicellular green alga, Chlamydomonas reinhardtii is a well-developed model organism [11] that has been widely used for the study of important cellular and metabolic processes such as photosynthesis, cell cycle, redox regulation, flagella biogenesis, or nitrogen metabolism,2.among others [12,13,14]
Summary
Eukaryotic cells are able to degrade intracellular material through a membrane-trafficking process known as autophagy This catabolic process allows cells to deliver cytosolic contents including proteins, membranes, and even organelles to the vacuole or lysosome. The ubiquitin-like protein ATG8 plays an important role in the processes of autophagosome formation, target recognition, and vacuole tethering [8,9]. The ATG4 protease from Chlamydomonas coordinately to accomplish vesicle (Trx) expansion, autophagosome formation, recognition and is activated by the thioredoxin system and reversibly inhibited by ROScargo or irreversibly autophagosome to the vacuole. RPS6 and RPL37 are engulfed autophagosome and targeted to the agents thioredoxin (Trx)proteins systemsuch andasreversibly inhibited by ROSby orthe irreversibly inactivated by blocking where they(IAM). RPL37 are engulfed by the autophagosome and targeted to the vacuole where they are degraded https://phytozome.jgi.doe.gov/pz/portal.html) of Chlamydomonas ATG proteins are: ATG1 and recycled.
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