ArticlePlant signaling & behavior2013
AtTPR7 as part of the Arabidopsis Sec post-translocon.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Volleying plasma membrane proteins from birth to death: Role of J-domain proteins.Frontiers in molecular biosciences · 2022Review
- Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways.Plant physiology · 2021Review
- AtSec62 is critical for plant development and is involved in ER-phagy in Arabidopsis thaliana.Journal of integrative plant biology · 2020Article
- Functional Diversification of ER Stress Responses in Arabidopsis.Trends in biochemical sciences · 2020Review
- Maintaining the factory: the roles of the unfolded protein response in cellular homeostasis in plants.The Plant journal : for cell and molecular biology · 2017Article
- Protein-protein interactions visualized by bimolecular fluorescence complementation in tobacco protoplasts and leaves.Journal of visualized experiments : JoVE · 2014Article
- Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The secretory system in eukaryotic organisms ensures targeting of proteins to their place of function after they entered the endoplasmic reticulum either co- or post-translationally. Thereby proteins are translocated through the Sec translocon into the endoplasmic reticulum. In the Arabidopsis genome homologs for the three major components of the Sec translocon, the central pore Sec61α and the auxiliary proteins Sec62 and Sec63 are present. Phylogenetic analyses show Sec61α to be the most conserved subunit within the Sec translocon whereas Sec62 and Sec63 show less homology but contain the same functional domains among all organisms. We recently characterized a novel tetratricopeptide repeat domain containing protein, AtTPR7, as part of the Arabidopsis Sec translocon which is probably involved in chaperone assisted post-translational import. In this study we investigated the interaction of AtTPR7 with Sec62 as well as the cytosolic chaperones HSP70 and HSP90 not only in vitro but also in vivo to further strengthen the hypothesis of AtTPR7 being a chaperone docking protein of the Sec translocon for secretory preproteins in Arabidopsis.
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