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G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling

Permanent lenke
https://hdl.handle.net/10037/21857
DOI
https://doi.org/10.1016/j.cell.2020.12.024
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Åpne
article.pdf (13.44Mb)
Publisert versjon (PDF)
Dato
2021-01-25
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Forfatter
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
Sammendrag
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 rapamycin complex 1 (mTORC1) by amino acids and insulin. Like the TSC complex, G3BP1 deficiency elicits phenotypes related to mTORC1 hyperactivity. In the context of tumors, low G3BP1 levels enhance mTORC1-driven breast cancer cell motility and correlate with adverse outcomes in patients. Furthermore, G3bp1 inhibition in zebrafish disturbs neuronal development and function, leading to white matter heterotopia and neuronal hyperactivity. Thus, G3BPs are not only core components of SGs but also a key element of lysosomal TSC-mTORC1 signaling.
Forlag
Elsevier
Sitering
Prentzell, Rehbein, Sandoval, De Meulemeester, Baumeister, Brohée, Berdel B, Bockwoldt M, Carroll B, Chowdhury, von Deimling A, Demetriades, Figlia, de Arauj, Heberle AM, Heiland I, Holzwarth, Huber, Jaworski J, Kedra, Kern, Kopach, Korolchuk VI, van't Land-Kuper, Macias, Nellist, Palm, Pusch S, Ramos Pittol, Reil, Reintjes, Reuter, Sampson JR, Scheldeman, Siekierska A, Stefan, Teleman, Thomas, Torres-Quesada, Trump S, West, de Witte P, Woltering, Yordanov, Zmorzynska, Opitz CA, Thedieck K. G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling. Cell. 2021;184:655-674
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