Measurement of the Activity of the Atg4 Cysteine Proteases

M. Li, Y. Fu, Z. Yang, X. M. Yin

Research output: Chapter in Book/Report/Conference proceedingChapter

7 Scopus citations

Abstract

While only one Atg4 is present in yeast, there are four Atg4 homologues in human and in mouse with different substrate specificities and catalytic efficiencies. The molecule Atg4 is a type of cysteine protease, and is known for its crucial roles in cleavage of the Atg8 family proteins before they can be conjugated to phospholipids, and also in cleavage of the conjugated Atg8 molecules from the membrane, a process known as deconjugation. Both processes are required for the maximal efficiency in autophagosome biogenesis. Atg4 could thus be a target for intervention of the autophagy process. It is thus important to measure Atg4 activity to determine and to modulate the autophagy function. Here, we review the catalytic functions and regulatory mechanisms of human Atg4 proteases and discuss the methodology for analyzing Atg4 activity in details.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages207-225
Number of pages19
DOIs
StatePublished - 2017

Publication series

NameMethods in Enzymology
Volume587
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Atg4
  • Atg8
  • Enzymatic kinetics
  • FRET
  • GABARAP
  • GATE-16
  • High-throughput screening
  • LC3

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Li, M., Fu, Y., Yang, Z., & Yin, X. M. (2017). Measurement of the Activity of the Atg4 Cysteine Proteases. In Methods in Enzymology (pp. 207-225). (Methods in Enzymology; Vol. 587). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2016.10.024