The Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability.

Abstract:

:Bulk degradation and nutrient recycling are events associated with autophagy. The core components of the autophagy machinery have been elucidated recently using molecular and genetic approaches. In particular, two ubiquitin-like proteins, ATG8 and ATG12, which conjugate with phosphatidylethanolamine (PE) and ATG5, respectively, forming ATG8-PE and ATG12-ATG5 complexes, were shown to be essential in autophagosome formation. Our recent findings reveal that the Arabidopsis thaliana acyl-CoA-binding protein ACBP3 binds the phospholipid PE in vitro and that ACBP3 overexpression and downregulation correlate with PE composition in rosettes. Furthermore, ACBP3-overexpressors (ACBP3-OEs) display accelerated salicylic acid-dependent leaf senescence resembling the phenotype of Arabidopsis knockout (KO) mutants defective in autophagy-related (ATG) proteins. Consistently, downregulation of ACBP3 (ACBP3-KOs) delays dark-induced leaf senescence. By analysis of transgenic Arabidopsis expressing GFP-ATG8e as well as those co-expressing ACBP3-OE and GFP-ATG8e, we showed that ACBP3-overexpression disrupts autophagosome formation and enhanced degradation of ATG8 under starvation conditions, suggesting that ACBP3 is an important regulator of the ATG8-PE complex via its interaction with PE. Here, a working model for the role of ACBP3 in the regulation of autophagy-mediated leaf senescence is presented.

journal_name

Autophagy

journal_title

Autophagy

authors

Xiao S,Chye ML

doi

10.1105/tpc.110.075333

subject

Has Abstract

pub_date

2010-08-01 00:00:00

pages

802-4

issue

6

eissn

1554-8627

issn

1554-8635

pii

12576

journal_volume

6

pub_type

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