Article
G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling.
Cell - 4 Feb 2021
Prentzell Mirja Tamara, Rehbein Ulrike, Cadena Sandoval Marti, De Meulemeester Ann-Sofie, Baumeister Ralf, Brohée Laura, Berdel Bianca, Bockwoldt Mathias, Carroll Bernadette, Chowdhury Suvagata Roy, von Deimling Andreas, Demetriades Constantinos, Figlia Gianluca, de Araujo Mariana Eca Guimaraes, Heberle Alexander M, Heiland Ines, Holzwarth Birgit, Huber Lukas A, Jaworski Jacek, Kedra Magdalena, Kern Katharina, Kopach Andrii, Korolchuk Viktor I, van 't Land-Kuper Ineke, Macias Matylda, Nellist Mark, Palm Wilhelm, Pusch Stefan, Ramos Pittol Jose Miguel, Reil Michèle, Reintjes Anja, Reuter Friederike, Sampson Julian R, Scheldeman Chloë, Siekierska Aleksandra, Stefan Eduard, Teleman Aurelio A, Thomas Laura E, Torres-Quesada Omar, Trump Saskia, West Hannah D, de Witte Peter, Woltering Sandra, Yordanov Teodor E, Zmorzynska Justyna, Opitz Christiane A, Thedieck Kathrin
Abstract excerpt
Ras GTPase-activating protein-binding proteins 1 and 2 (G3BP1 and G3BP2, respectively) are widely recognized as core components of stress granules (SGs). We report that G3BPs reside at the cytoplasmic surface of lysosomes. They act in a non-redundant manner to anchor the tuberous sclerosis complex (TSC) protein complex to lysosomes and suppress activation of the metabolic master regulator mechanistic target of...
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