Blar i forfatter "Carroll, Bernadette"

Viser treff 1-2 av 2

    • G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling 

      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 ...

    • SQSTM1/p62 mediates crosstalk between autophagy and the UPS in DNA repair 

      Hewitt, Graeme; Carroll, Bernadette; Sarallah, Rezazadeh; Correia-Melo, Clara; Ogrodnik, Mikolaj; Nelson, Glyn; Otten, Elsje G; Manni, Diego; Antrobus, Robin; Morgan, Brian A; von Zglinicki, Thomas; Jurk, Diana; Seluanov, Andrei; Gorbunova, Vera; Johansen, Terje; Passos, João F; Korolchuk, Viktor I (Journal article; Tidsskriftartikkel; Peer reviewed, 2016-08-23)
      SQSTM1/p62 (sequestosome 1) selectively targets polyubiquitinated proteins for degradation via macroautophagy and the proteasome. Additionally, SQSTM1 shuttles between the cytoplasmic and nuclear compartments, although its role in the nucleus is relatively unknown. Here, we report that SQSTM1 dynamically associates with DNA damage foci (DDF) and regulates DNA repair. Upon induction of DNA damage ...