The ESCRT-III-interacting deubiquitinating enzyme AMSH3 is essential for degradation of ubiquitinated membrane proteins in Arabidopsis thaliana.
Plant Cell Physiol
; 55(4): 727-36, 2014 Apr.
Article
in En
| MEDLINE
| ID: mdl-24486765
ABSTRACT
Post-translational modification by ubiquitin plays a key role in the regulation of endocytic degradation in which ubiquitinated plasma membrane cargos are transported to the vacuole for degradation dependent on the ESCRT (endosomal sorting complex required for transport) machinery. Arabidopsis AMSH3 (ASSOCIATED MOLECULE WITH THE SH3 DOMAIN OF STAM 3) is a deubiquitinating enzyme that interacts with at least two subunits of the ESCRT-III machinery, VPS2.1 and VPS24.1. amsh3 null mutation causes seedling lethality, and amsh3 null mutants show defects in multiple intracellular trafficking pathways. In this study, we further analyzed the amsh3 mutant phenotype and showed that amsh3 accumulates membrane-associated ubiquitinated proteins, supporting the indication that AMSH3 functions in ubiquitin-mediated endocytic degradation. In accordance with this, an enzymatic inactive variant of AMSH3 inhibits the AvrPtoB-dependent endocytic degradation of CERK1 (CHITIN ELICITOR RECEPTOR KINASE 1). Furthermore, we showed that the interaction of AMSH3 with ESCRT-III is important for its function in planta. Together, our data indicate the importance of AMSH3 and the AMSH3-ESCRT-III interaction for deubiquitination and degradation of ubiquitinated membrane substrates in plants.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arabidopsis
/
Arabidopsis Proteins
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Endosomal Sorting Complexes Required for Transport
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Ubiquitinated Proteins
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Proteolysis
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Ubiquitin-Specific Proteases
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Membrane Proteins
Language:
En
Journal:
Plant Cell Physiol
Journal subject:
BOTANICA
Year:
2014
Document type:
Article
Affiliation country:
Alemania