The TPLATE adaptor complex drives clathrin-mediated endocytosis in plants Journal Article

Author(s): Gadeyne, Astrid; Sánchez-Rodríguez, Clara; Vanneste, Steffen; Di Rubbo, Simone; Zauber, Henrik; Vanneste, Kevin; Van Leene, Jelle; De Winne, Nancy; Eeckhout, Dominique; Persiau, Geert; Van De Slijke, Eveline; Cannoot, Bernard; Vercruysse, Leen; Mayers, Jonathan R; Adamowski, Maciej; Kania, Urszula; Ehrlich, Matthias; Schweighofer, Alois; Ketelaar, Tijs; Maere, Steven; Bednarek, Sebastian Y; Friml, Jiří; Gevaert, Kris; Witters, Erwin; Russinova, Eugenia; Persson, Staffan; De Jaeger, Geert; Van Damme, Daniël
Article Title: The TPLATE adaptor complex drives clathrin-mediated endocytosis in plants
Affiliation IST Austria
Abstract: Clathrin-mediated endocytosis is the major mechanism for eukaryotic plasma membrane-based proteome turn-over. In plants, clathrin-mediated endocytosis is essential for physiology and development, but the identification and organization of the machinery operating this process remains largely obscure. Here, we identified an eight-core-component protein complex, the TPLATE complex, essential for plant growth via its role as major adaptor module for clathrin-mediated endocytosis. This complex consists of evolutionarily unique proteins that associate closely with core endocytic elements. The TPLATE complex is recruited as dynamic foci at the plasma membrane preceding recruitment of adaptor protein complex 2, clathrin, and dynamin-related proteins. Reduced function of different complex components severely impaired internalization of assorted endocytic cargoes, demonstrating its pivotal role in clathrin-mediated endocytosis. Taken together, the TPLATE complex is an early endocytic module representing a unique evolutionary plant adaptation of the canonical eukaryotic pathway for clathrin-mediated endocytosis.
Journal Title: Cell
Volume: 156
Issue 4
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2014-02-13
Start Page: 691
End Page: 704
DOI: 10.1016/j.cell.2014.01.039
Notes: The authors would like to thank Wim Grunewald (VIB/UGent, Belgium), Niko Geldner (University of Lausanne, Switzerland), Satoshi Naramoto and Masaru Fujimoto (University of Tokyo, Japan), Inhwan Hwang (Pohang University, Korea), Gerd Jürgens (Tübingen University, Germany), and Christian Luschnig (Vienna University, Austria) for sharing materials; Mansour Karimi and Riet De Rycke (VIB/University of Ghent, Belgium) for vector cloning and IEM attempts; and Luis Vidali (Worchester Polytechnic Institute, USA) for constructive discussions. A.G. was indebted to the Agency for Innovation by Science and Technology for a predoctoral fellowship. S.P. and C.S.R were funded through the Max-Planck Gesellschaft. K.V., S.V., J.V.L. and S.M. are fellows of the Research Foundation - Flanders (FWO). S.D.R. was funded by the Marie-Curie Initial Training Network BRAVISSIMO (PITN-GA-2008-215118). J.R.M and S.Y.B were supported by the National Science Foundation (1121998) (S.Y.B.). Part of this work was carried out using the Stevin Supercomputer Infrastructure at Ghent University, funded by Ghent University, the Hercules Foundation, and the Flemish Government–department EWI. We apologize to colleagues whose work could not be cited due to space limitations.
Open access: no