Prentzell, Mirja Tamara; Rehbein, Ulrike; Sandoval, Marti Cadena; 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 Arauj, Mariana Eca Guimaraes; Heberle, Alexander Martin; 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 (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-01-25)
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 ...
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