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The endocytic TPLATE complex internalizes ubiquitinated plasma membrane cargo
- 1.0566856 - ÚEB 2023 RIV GB eng J - Článek v odborném periodiku
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
Grant CEP: GA ČR(CZ) GM22-35680M
Institucionální podpora: RVO:61389030
Klíčová slova: Cell Membrane * Clathrin * Endocytosis
Obor OECD: Cell biology
Impakt faktor: 18, rok: 2022
Způsob publikování: 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.
Trvalý link: https://hdl.handle.net/11104/0338124
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