The TPLATE complex (TPC) is an ancient multi-subunit adaptor complex, essential for clathrin-mediated endocytosis in plants. We found that the evolutionary specific SH3 domain on the large TPC subunit, TASH3, recognizes ubiquitinated cargo proteins at the plasma membrane, providing a link between endocytosis and internalization of ubiquitinated proteins.
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References
Arora, D. & Van Damme, D. Motif-based endomembrane trafficking. Plant Physiol. 186, 221–238 (2021). A review article that gives an overview on protein trafficking, adaptor complexes and cargo recognition motifs.
Gadeyne, A. et al. The TPLATE adaptor complex drives clathrin-mediated endocytosis in plants. Cell 156, 691–704 (2014). This study identifies the TPC and provides mechanistic insight into its function during clathrin-mediated endocytosis in Arabidopsis.
Wang, P. et al. Plant AtEH/Pan1 proteins drive autophagosome formation at ER–PM contact sites with actin and endocytic machinery. Nat. Commun. 10, 5132 (2019). This paper reports on the involvement of the TPC in the formation of autophagosomes at endoplasmic reticulum–PM contact sites.
Claus, L. A. N. et al. Phosphorylation and ubiquitination independent endocytosis of BRI1. Preprint at bioRxiv https://doi.org/10.1101/2022.07.11.499622 (2022). This article reports that BRI1 can be internalized via parallel endocytic routes and machineries.
Liu, D. et al. Endocytosis of BRASSINOSTEROID INSENSITIVE1 is partly driven by a canonical Tyr-based motif. Plant Cell 32, 3598–3612 (2020). This paper demonstrates that canonical AP-2 recognition motifs of BRI1 contribute to its internalization. However, mutating these motifs does not abolish BRI1 internalization.
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This is a summary of: Grones, P. et al. The endocytic TPLATE complex internalizes ubiquitinated plasma mebrane cargo. Nat. Plants https://doi.org/10.1038/s41477-022-01280-1 (2022).
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Ubiquitinated plasma membrane proteins are specifically recognized by the TPLATE complex. Nat. Plants 8, 1339–1340 (2022). https://doi.org/10.1038/s41477-022-01290-z
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DOI: https://doi.org/10.1038/s41477-022-01290-z
