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Tagged ATG8-Coding Constructs for the In Vitro and In Vivo Assessment of ATG4 Activity

López-Otín, C., Mariño, G.·2017·Methods in Enzymology
DOI 10.1016/bs.mie.2016.11.001
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Abstract

Autophagy is a catabolic pathway, which mediates the degradation of cytoplasmic components and sustains many essential cellular functions. More than 30 genes have been involved in different aspects of this essential process in simple eukaryotes as yeast. Among these genes, those coding for members of the Atg4-Atg8 proteolytic system have acquired a high degree of complexity throughout evolution. Contrasting with the situation in unicellular eukaryotes, in which the system is composed by just a single protease (Atg4) and a single substrate (Atg8), evolution has led to the presence of several members for both Atg4 and Atg8 families in multicellular organisms. In human cells, there are four Atg4 proteases and six Atg8 substrates, which have probably evolved to cope with specific requirements for autophagic pathway in more complex scenarios. Despite these considerations, the reasons for the evolutionarily acquired complexity of this proteolytic system are still not completely understood. In this work, we describe two different applications of a relatively simple but useful technique to analyze protease-substrate specificity of this system in mammalian cells. By using the described technique, it is possible to determine the cellular efficiency in the initial cleavage for each of the Atg8 family members in diverse experimental settings both in cultured cells and live laboratory mice.

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Research works printed but not linked: 28

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Metadata

Authors
López-Otín, C., & Mariño, G.
Venue
Methods in Enzymology
Publisher
Elsevier
Published
2017
Pages
189-205
ISSN
0076-6879
DOI
10.1016/bs.mie.2016.11.001
Cited by
4
References
4
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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López-Otín, C., & Mariño, G. (2017). Tagged ATG8-Coding Constructs for the In Vitro and In Vivo Assessment of ATG4 Activity. Methods in Enzymology. https://doi.org/10.1016/bs.mie.2016.11.001