Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Intracellular Membranes/metabolism"'
Publikováno v:
The Journal of Cell Biology, 2001 Nov 01. 155(4), 593-604.
Externí odkaz:
https://www.jstor.org/stable/1620723
Autor:
Hector Foronda, Yangxue Fu, Adriana Covarrubias-Pinto, Hartmut T. Bocker, Alexis González, Eric Seemann, Patricia Franzka, Andrea Bock, Ramachandra M. Bhaskara, Lutz Liebmann, Marina E. Hoffmann, Istvan Katona, Nicole Koch, Joachim Weis, Ingo Kurth, Joseph G. Gleeson, Fulvio Reggiori, Gerhard Hummer, Michael M. Kessels, Britta Qualmann, Muriel Mari, Ivan Dikić, Christian A. Hübner
Publikováno v:
Nature
Foronda, H, Fu, Y, Covarrubias-Pinto, A, Bocker, H T, González, A, Seemann, E, Franzka, P, Bock, A, Bhaskara, R M, Liebmann, L, Hoffmann, M E, Katona, I, Koch, N, Weis, J, Kurth, I, Gleeson, J G, Reggiori, F, Hummer, G, Kessels, M M, Qualmann, B, Mari, M, Dikić, I & Hübner, C A 2023, ' Heteromeric clusters of ubiquitinated ER-shaping proteins drive ER-phagy ', Nature, vol. 618, no. 7964, pp. 402-410 . https://doi.org/10.1038/s41586-023-06090-9
Foronda, H, Fu, Y, Covarrubias-Pinto, A, Bocker, H T, González, A, Seemann, E, Franzka, P, Bock, A, Bhaskara, R M, Liebmann, L, Hoffmann, M E, Katona, I, Koch, N, Weis, J, Kurth, I, Gleeson, J G, Reggiori, F, Hummer, G, Kessels, M M, Qualmann, B, Mari, M, Dikić, I & Hübner, C A 2023, ' Heteromeric clusters of ubiquitinated ER-shaping proteins drive ER-phagy ', Nature, vol. 618, no. 7964, pp. 402-410 . https://doi.org/10.1038/s41586-023-06090-9
Membrane-shaping proteins characterized by reticulon homology domains play an important part in the dynamic remodelling of the endoplasmic reticulum (ER). An example of such a protein is FAM134B, which can bind LC3 proteins and mediate the degradatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::587ec4f4d78e10eb10e252a8fb732491
https://doi.org/10.1038/s41586-023-06090-9
https://doi.org/10.1038/s41586-023-06090-9
Publikováno v:
Nature Communications. 13(1)
The protein kinase mechanistic target of rapamycin complex 1 (mTORC1) is a master regulator of cell growth and proliferation, supporting anabolic reactions and inhibiting catabolic pathways like autophagy. Its hyperactivation is a frequent event in c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dris___00893::c7015ff21183a55e9e73de884b7c95cd
https://doi.org/10.1038/s41467-022-32487-7
https://doi.org/10.1038/s41467-022-32487-7
Autor:
Kaeser-Pebernard, Stephanie, Vionnet, Christine, Mari, Muriel, Sankar, Devanarayanan Siva, Hu, Zehan, Roubaty, Carole, Martinez-Martinez, Esther, Zhao, Huiyuan, Spuch-Calvar, Miguel, Petri-Fink, Alke, Rainer, Gregor, Steinberg, Florian, Reggiori, Fulvio, Dengjel, Joern
Publikováno v:
Kaeser-Pebernard, S, Vionnet, C, Mari, M, Sankar, D S, Hu, Z, Roubaty, C, Martínez-Martínez, E, Zhao, H, Spuch-Calvar, M, Petri-Fink, A, Rainer, G, Steinberg, F, Reggiori, F & Dengjel, J 2022, ' mTORC1 controls Golgi architecture and vesicle secretion by phosphorylation of SCYL1 ', Nature Communications, vol. 13, no. 1, 4685 . https://doi.org/10.1038/s41467-022-32487-7
Nature Communications, 13(1). Nature Publishing Group
Nature Communications, 13(1):4685. Nature Publishing Group
Nature Communications, 13(1). Nature Publishing Group
Nature Communications, 13(1):4685. Nature Publishing Group
mTORC1 is a master regulator of cell growth with well-known functions in inhibiting autophagic vesicle formation. Here, the authors show that mTORC1 also affects Golgi architecture and vesicle secretion by phosphorylating the scaffold protein SCYL1.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0b6a00518154df4ad35bfaf4aade0ea4
https://pure.au.dk/portal/da/publications/mtorc1-controls-golgi-architecture-and-vesicle-secretion-by-phosphorylation-of-scyl1(32310649-10bb-427b-934c-d6c8be6b1464).html
https://pure.au.dk/portal/da/publications/mtorc1-controls-golgi-architecture-and-vesicle-secretion-by-phosphorylation-of-scyl1(32310649-10bb-427b-934c-d6c8be6b1464).html
Autor:
Herre Jelger Risselada, Andreas Mayer
Publikováno v:
The Biochemical journal, vol. 477, no. 1, pp. 243-258
Physiological membrane vesicles are built to separate reaction spaces in a stable manner, even when they accidentally collide or are kept in apposition by spatial constraints in the cell. This requires a natural resistance to fusion and mixing of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f171a5c59d98e083e3ff7574043784dd
https://doi.org/10.1042/bcj20190050
https://doi.org/10.1042/bcj20190050
Autor:
Corinne Sagné, Bruno Gasnier, Christopher Ribes, Quentin Verdon, Michel Jadot, Marielle Boonen
Publikováno v:
Verdon, Q, Boonen, M, Ribes, C, Jadot, M, GASNIER, B & Sagné, C 2017, ' SNAT7 is the primary lysosomal glutamine exporter required for extracellular protein-dependent growth of cancer cells ', Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 18, pp. E3602-E3611 . https://doi.org/10.1073/pnas.1617066114
Lysosomes degrade cellular components sequestered by autophagy or extracellular material internalized by endocytosis and phagocytosis. The macromolecule building blocks released by lysosomal hydrolysis are then exported to the cytosol by lysosomal tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f628eaa098d558b69a8f7164a637131
https://researchportal.unamur.be/en/publications/d31f8ac5-cf98-4ab4-80d7-38e70cfcd976
https://researchportal.unamur.be/en/publications/d31f8ac5-cf98-4ab4-80d7-38e70cfcd976
Autor:
Julie Meurisse, Ramona Schuster, Chen Bibi, Lodewijk IJlst, Nadav Shai, Nir Cohen, Muriel Mari, Einat Zalckvar, Mafalda Escobar-Henriques, Hans R. Waterham, Adam Hughes, Laetitia Cavellini, Eden Yifrach, Mickael M. Cohen, Maya Schuldiner, Carlo W.T. van Roermund, Ronald J.A. Wanders, Lior Zada, Fulvio Reggiori
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2018, 9, pp.1761. ⟨10.1038/s41467-018-03957-8⟩
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature communications, 9(1):1761. Nature Publishing Group
Shai, N, Yifrach, E, van Roermund, C W T, Cohen, N, Bibi, C, IJlst, L, Cavellini, L, Meurisse, J, Schuster, R, Zada, L, Mari, M C, Reggiori, F M, Hughes, A L, Escobar-Henriques, M, Cohen, M M, Waterham, H R, Wanders, R J A, Schuldiner, M & Zalckvar, E 2018, ' Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact ', Nature Communications, vol. 9, no. 1, pp. 1761 . https://doi.org/10.1038/s41467-018-03957-8
Nature Communications, 9(1):1761. Nature Publishing Group
Nature Communications, Nature Publishing Group, 2018, 9, pp.1761. ⟨10.1038/s41467-018-03957-8⟩
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature communications, 9(1):1761. Nature Publishing Group
Shai, N, Yifrach, E, van Roermund, C W T, Cohen, N, Bibi, C, IJlst, L, Cavellini, L, Meurisse, J, Schuster, R, Zada, L, Mari, M C, Reggiori, F M, Hughes, A L, Escobar-Henriques, M, Cohen, M M, Waterham, H R, Wanders, R J A, Schuldiner, M & Zalckvar, E 2018, ' Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact ', Nature Communications, vol. 9, no. 1, pp. 1761 . https://doi.org/10.1038/s41467-018-03957-8
Nature Communications, 9(1):1761. Nature Publishing Group
The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04e072777b98620ce047b021657bd05d
https://doi.org/10.1038/s41467-018-03957-8
https://doi.org/10.1038/s41467-018-03957-8
Autor:
Lloyd-Lewis, Bethan, Krueger, Caroline C, Sargeant, Timothy J, D'Angelo, Michael E, Deery, Michael J, Feret, Renata, Howard, Julie A, Lilley, Kathryn S, Watson, Christine J
Publikováno v:
Lloyd-Lewis, B, Krueger, C C, Sargeant, T J, D'Angelo, M E, Deery, M J, Feret, R, Howard, J A, Lilley, K S & Watson, C J 2018, ' Stat3-mediated alterations in lysosomal membrane protein composition ', Journal of Biological Chemistry, vol. 293, no. 12, pp. 4244-4261 . https://doi.org/10.1074/jbc.RA118.001777
Lysosome function is essential in cellular homeostasis. In addition to its recycling role, the lysosome has recently been recognized as a cellular signaling hub. We have shown in mammary epithelial cells, both in vivo and in vitro, that signal transd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::068f05195a24e26484b273a5f17e844e
Autor:
Judith Klumperman, Fulvio Reggiori, Muriel Mari, Yingying Cong, Tineke Veenendaal, Xingdong Zhou, Dongfang Shi
Publikováno v:
Viruses [E], 9(9). Multidisciplinary Digital Publishing Institute (MDPI)
Viruses
Viruses, 9(9):251. MDPI AG
Viruses, Vol 9, Iss 9, p 251 (2017)
Zhou, X, Cong, Y, Veenendaal, T, Klumperman, J, Shi, D, Mari, M & Reggiori, F 2017, ' Ultrastructural Characterization of Membrane Rearrangements Induced by Porcine Epidemic Diarrhea Virus Infection ', Viruses, vol. 9, no. 9 . https://doi.org/10.3390/v9090251
Viruses; Volume 9; Issue 9; Pages: 251
Viruses
Viruses, 9(9):251. MDPI AG
Viruses, Vol 9, Iss 9, p 251 (2017)
Zhou, X, Cong, Y, Veenendaal, T, Klumperman, J, Shi, D, Mari, M & Reggiori, F 2017, ' Ultrastructural Characterization of Membrane Rearrangements Induced by Porcine Epidemic Diarrhea Virus Infection ', Viruses, vol. 9, no. 9 . https://doi.org/10.3390/v9090251
Viruses; Volume 9; Issue 9; Pages: 251
The porcine epidemic diarrhea virus (PEDV) is a coronavirus (CoV) belonging to the alpha-CoV genus and it causes high mortality in infected sucking piglets, resulting in substantial losses in the farming industry. CoV trigger a drastic reorganization
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::655b7619079d483a24ae3faa8ae8b7bf
https://dspace.library.uu.nl/handle/1874/354491
https://dspace.library.uu.nl/handle/1874/354491
Autor:
Tony A. Rodrigues, Aurora Barros-Barbosa, Ana G. Pedrosa, Jorge E. Azevedo, Ana F. Dias, Tânia Francisco
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates. This import involves binding of newly synthesized proteins by cytosolic peroxisomal biogenesis factor 5 (PEX
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f48b33e77a0947decee710e624b6ca2
https://europepmc.org/articles/PMC5602389/
https://europepmc.org/articles/PMC5602389/