ArticlePlant signaling & behavior2013
The Arabidopsis exocyst subcomplex subunits involved in a golgi-independent transport into the vacuole possess consensus autophagy-associated atg8 interacting motifs.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape.Nature plants · 2025Article
- MpPUB9, a U-box E3 ubiquitin ligase, acts as a positive regulator by promoting the turnover of MpEXO70.1 under high salinity in Marchantia polymorpha.The New phytologist · 2024Article
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Exocyst subunit Exo70B2 is linked to immune signaling and autophagy.The Plant cell · 2021Article
- Review
- Multiple Functions of ATG8 Family Proteins in Plant Autophagy.Frontiers in cell and developmental biology · 2020Review
- Recent Advances in Membrane Shaping for Plant Autophagosome Biogenesis.Frontiers in plant science · 2020Review
- New advances in autophagy in plants: Regulation, selectivity and function.Seminars in cell & developmental biology · 2018Review
- Article
- Article
- Constitutive Negative Regulation of R Proteins in Arabidopsis also via Autophagy Related Pathway?Frontiers in plant science · 2016Article
- Unconventional protein secretion in plants: a critical assessment.Protoplasma · 2016Review
- Old AIMs of the exocyst: evidence for an ancestral association of exocyst subunits with autophagy-associated Atg8 proteins.Plant signaling & behavior · 2013Article
Corrections and comments
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Authors and funding
2 authors.
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Abstract
The exocyst complex is a multi-subunits evolutionary conserved complex, which was originally shown to be primarily associated with vesicular transport to the plasma membrane. A recent report (Kulich et al., 2013 Traffic; In Press) revealed that AtEXO70B1, one of the multiple subunits of the exocyst complex of Arabidopsis thaliana plants, is co-transported with the autophagy-associated Atg8f protein to the vacuole. This pathway does not involve the Golgi apparatus. The co-localization of AtEXO70B1 and Atg8f suggests either that both of these proteins are co-transported together to the vacuole or, alternatively, that Atg8 binds to a putative Atg8 interacting motif (AIM) located within the AtEXO70B1 polypeptide, apparently forming a tethering complex for an autophagic complex that is transported to the vacuole. In the present addendum, by tooling a bioinformatics approach, we show that AtEXO70B1 as well as the additional 20 paralogs of Arabidopsis EXO70 exocyst subunits each possess one or more AIMs whose consensus sequence implies their high fidelity binding to Atg8. This indicates that the autophagy machinery is strongly involved in the assembly, transport, and apparently also the function of AtEXO70B1 as well as the exocyst sub complex.
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