A close-up view of membrane contact sites between the endoplasmic reticulum and the endolysosomal system: From yeast to man

Autor(en): Hoenscher, Carina
Ungermann, Christian 
Stichwörter: ARMADILLO-REPEAT PROTEIN; Biochemistry & Molecular Biology; Endosome; ER; membrane contact site; MITOCHONDRIAL MORPHOLOGY; nuclear endoplasmic reticulum; NUCLEUS-VACUOLE JUNCTIONS; OXYSTEROL-BINDING-PROTEIN; PIECEMEAL MICROAUTOPHAGY; PLASMA-MEMBRANE; SACCHAROMYCES-CEREVISIAE; STRUCTURAL BASIS; tether; TETHERING COMPLEXES; vacuole
Erscheinungsdatum: 2014
Herausgeber: TAYLOR & FRANCIS LTD
Journal: CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volumen: 49
Ausgabe: 3
Startseite: 262
Seitenende: 268
Zusammenfassung: 
Maintenance of organelle identity is crucial for the functionality of eukaryotic cells. Hence, transfer reactions between different compartments must be highly efficient and tightly regulated at the same time. Membrane contact sites (MCSs) represent an important route for inter-organelle transport and communication independent of vesicular trafficking. Due to extensive research, the mechanistic understanding of these sites increases constantly. However, how the formation and the versatile functions of MCSs are regulated is mainly unclear. Within this review, we focus on one well-known MCS, the nucleus-vacuole junction in yeast and discuss its analogy to endoplasmic reticulum-late endosome contacts in metazoan. Formation of the junction in yeast requires Vac8, a protein that is involved in various cellular processes at the yeast vacuole and a target of multiple posttranslational modifications. We discuss the possibility that dual functionality of proteins involved in contact formation is a common principle to coordinate inter-organelle transfer with organellar biogenesis.
ISSN: 10409238
DOI: 10.3109/10409238.2013.875512

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