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Lam6 Regulates the Extent of Contacts between Organelles.
Elbaz-Alon, Yael; Eisenberg-Bord, Michal; Shinder, Vera; Stiller, Sebastian Berthold; Shimoni, Eyal; Wiedemann, Nils; Geiger, Tamar; Schuldiner, Maya.
Afiliación
  • Elbaz-Alon Y; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Eisenberg-Bord M; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Shinder V; Department of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Stiller SB; Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung (ZBMZ), Universität Freiburg, Freiburg 79104, Germany; Fakultät für Biologie, Universität Freiburg, Freiburg 79104, Germany.
  • Shimoni E; Department of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
  • Wiedemann N; Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung (ZBMZ), Universität Freiburg, Freiburg 79104, Germany; BIOSS Centre for Biological Signalling Studies, Universität Freiburg, Freiburg 79104, Germany.
  • Geiger T; Department of Human Molecular Genetics and Biochemistry, Tel-Aviv University, Tel Aviv 6997801, Israel.
  • Schuldiner M; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: maya.schuldiner@weizmann.ac.il.
Cell Rep ; 12(1): 7-14, 2015 Jul 07.
Article en En | MEDLINE | ID: mdl-26119743
ABSTRACT
Communication between organelles is crucial for eukaryotic cells to function as one coherent unit. An important means of communication is through membrane contact sites, where two organelles come into close proximity allowing the transport of lipids and small solutes between them. Contact sites are dynamic in size and can change in response to environmental or cellular stimuli; however, how this is regulated has been unclear. Here, we show that Saccharomyces cerevisiae Lam6 resides in several central contact sites ERMES (ER/mitochondria encounter structure), vCLAMP (vacuole and mitochondria patch), and NVJ (nuclear vacuolar junction). We show that Lam6 is sufficient for expansion of contact sites under physiological conditions and necessary for coordination of contact site size. Given that Lam6 is part of a large protein family and is conserved in vertebrates, our work opens avenues for investigating the underlying principles of organelle communication.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Vacuolas / Núcleo Celular / Antiportadores / Proteínas de Saccharomyces cerevisiae / Retículo Endoplásmico / Mitocondrias Idioma: En Revista: Cell Rep Año: 2015 Tipo del documento: Article País de afiliación: Israel

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Vacuolas / Núcleo Celular / Antiportadores / Proteínas de Saccharomyces cerevisiae / Retículo Endoplásmico / Mitocondrias Idioma: En Revista: Cell Rep Año: 2015 Tipo del documento: Article País de afiliación: Israel