The endocytic TPLATE complex internalizes ubiquitinated plasma membrane cargo

0566856 - ÚEB 2023 RIV GB eng J - Journal Article
Grones, P. - De Meyer, A. - Pleskot, Roman - Mylle, E. - Kraus, M. - Vandorpe, M. - Yperman, K. - Eeckhout, D. - Dragwidge, J. M. - Jiang, Q. - Nolf, J. - Pavie, B. - De Jaeger, G. - De Rybel, B. - Van Damme, D.
The endocytic TPLATE complex internalizes ubiquitinated plasma membrane cargo.
Nature Plants. Roč. 8, č. 12 (2022), s. 1467-1483. ISSN 2055-026X. E-ISSN 2055-0278
R&D Projects: GA ČR(CZ) GM22-35680M
Institutional support: RVO:61389030
Keywords : Cell Membrane * Clathrin * Endocytosis
OECD category: Cell biology
Impact factor: 18, year: 2022
Method of publishing: Open access
https://doi.org/10.1038/s41477-022-01280-1

Endocytosis controls the perception of stimuli by modulating protein abundance at the plasma membrane. In plants, clathrin-mediated endocytosis is the most prominent internalization pathway and relies on two multimeric adaptor complexes, the AP-2 and the TPLATE complex (TPC). Ubiquitination is a well-established modification triggering endocytosis of cargo proteins, but how this modification is recognized to initiate the endocytic event remains elusive. Here we show that TASH3, one of the large subunits of TPC, recognizes ubiquitinated cargo at the plasma membrane via its SH3 domain-containing appendage. TASH3 lacking this evolutionary specific appendage modification allows TPC formation but the plants show severely reduced endocytic densities, which correlates with reduced endocytic flux. Moreover, comparative plasma membrane proteomics identified differential accumulation of multiple ubiquitinated cargo proteins for which we confirm altered trafficking. Our findings position TPC as a key player for ubiquitinated cargo internalization, allowing future identification of target proteins under specific stress conditions.
Permanent Link: https://hdl.handle.net/11104/0338124