The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation.

Abstract:

:Autophagy is a bulk degradation process conserved among eukaryotes. In macro-autophagy, autophagosomes sequester cytoplasmic components and deliver their contents to lysosomes/vacuoles. Autophagosome formation requires the conjugation of Atg8, a ubiquitin-like protein, to phosphatidylethanolamine (PE). Here we report that the amino (N)-terminal region of Atg3, an E2-like enzyme for Atg8, plays a crucial role in Atg8-PE conjugation. The conjugating activities of Atg3 mutants lacking the 7 N-terminal amino acid residues or containing a Leu-to-Asp mutation at position 6 were severely impaired both in vivo and in vitro. In addition, the amino-terminal region is critical for interaction with the substrate, PE.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hanada T,Satomi Y,Takao T,Ohsumi Y

doi

10.1016/j.febslet.2009.03.009

subject

Has Abstract

pub_date

2009-04-02 00:00:00

pages

1078-83

issue

7

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00182-3

journal_volume

583

pub_type

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