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Akademický článek

Structure of the endosomal CORVET tethering complex

Autor: Dmitry Shvarev, Caroline König, Nicole Susan, Lars Langemeyer, Stefan Walter, Angela Perz, Florian Fröhlich, Christian Ungermann, Arne Moeller

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)

Abstract Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by

Externí odkaz: https://doaj.org/article/18ffc3ab95944c89abfd2dfd1e010c93

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Akademický článek

Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery

Autor: Dmitry Shvarev, Jannis Schoppe, Caroline König, Angela Perz, Nadia Füllbrunn, Stephan Kiontke, Lars Langemeyer, Dovile Januliene, Kilian Schnelle, Daniel Kümmel, Florian Fröhlich, Arne Moeller, Christian Ungermann

Publikováno v: eLife, Vol 11 (2022)

Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the mem

Externí odkaz: https://doaj.org/article/def295925ee6473dbd2d3883d11521f1

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Akademický článek

A conserved and regulated mechanism drives endosomal Rab transition

Autor: Lars Langemeyer, Ann-Christin Borchers, Eric Herrmann, Nadia Füllbrunn, Yaping Han, Angela Perz, Kathrin Auffarth, Daniel Kümmel, Christian Ungermann

Publikováno v: eLife, Vol 9 (2020)

Endosomes and lysosomes harbor Rab5 and Rab7 on their surface as key proteins involved in their identity, biogenesis, and fusion. Rab activation requires a guanine nucleotide exchange factor (GEF), which is Mon1-Ccz1 for Rab7. During endosome maturat

Externí odkaz: https://doaj.org/article/565a34edef7e4052a6e9c8fc62e3ccc1

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Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery

Autor: Caroline König, Jannis Schoppe, Dmitry Shvarev, Angela Perz, Nadia Füllbrunn, Stephan Kiontke, Lars Langemeyer, Dovile Januliene, Kilian Schnelle, Daniel Kümmel, Florian Fröhlich, Arne Moeller, Christian Ungermann

Publikováno v: eLife 11, e80901 (2022). doi:10.7554/eLife.80901

eLife 11, e80901 (2022). doi:10.7554/eLife.80901
Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and patho-genic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requiresHOPS, a c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5cdbb1f3709575f8990ebf950ccab91
https://doi.org/10.7554/elife.80901

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Structure of the lysosomal membrane fusion machinery

Lysosomes are of central importance in cellular recycling, nutrient signaling1,2and endocytosis, and are tightly connected to autophagy3and the invasion of pathogenic bacteria and viruses1,4. Lysosomal fusion events are fundamental to cell survival a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::307e8df90ee9b4872378c20d7f1bfb45
https://doi.org/10.1101/2022.05.05.490745

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Flexible open conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi

Autor: Yaping Han, Jannis Schoppe, Heike Stephanowitz, Angela Perz, Amir Apelbaum, Oliver Hofnagel, Jacob Piehler, Fan Liu, Christian Ungermann, Stefan Raunser, Evelyn Schubert, Oliver Birkholz, Erdal Yavavli

Publikováno v: The Journal of Biological Chemistry

Vesicle formation at endomembranes requires the selective concentration of cargo by coat proteins. Conserved adapter protein complexes at the Golgi (AP-3), the endosome (AP-1), or the plasma membrane (AP-2) with their conserved core domain and flexib

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cba2b369c182db77a3847ecec46c321c
https://pubmed.ncbi.nlm.nih.gov/34902351

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