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

Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code

Autor: Eric Herrmann, Lars Langemeyer, Kathrin Auffarth, Christian Ungermann, Daniel Kümmel

Publikováno v: J Biol Chem

Activation of the small GTPase Rab7 by its cognate guanine nucleotide exchange factor Mon1-Ccz1 (MC1) is a key step in the maturation of endosomes and autophagosomes. This process is tightly regulated and subject to precise spatiotemporal control of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dc29e5e498ff70968cb57eedfba138f
https://doi.org/10.1101/2022.08.14.503906

AP‐3 vesicle uncoating occurs after HOPS‐dependent vacuole tethering

Autor: Christian Ungermann, Kathrin Auffarth, Muriel Mari, Margarita Cabrera, Erdal Yavavli, Florian Fröhlich, Jannis Schoppe, Stefan Walter

Publikováno v: The EMBO Journal
EMBO Journal, 39(20):e105117. Wiley

Heterotetrameric adapter (AP) complexes cooperate with the small GTPase Arf1 or lipids in cargo selection, vesicle formation, and budding at endomembranes in eukaryotic cells. While most AP complexes also require clathrin as the outer vesicle shell,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfa74123c927694dd3a1219ef48e74b0
http://europepmc.org/articles/PMC7560216

Author response: A conserved and regulated mechanism drives endosomal Rab transition

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::de00278de72396a84af71dbd5c9761ac
https://doi.org/10.7554/elife.56090.sa2

Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites

Autor: Florian Fröhlich, Martin van der Laan, Christian Ungermann, Thomas Becker, Carina Hönscher, Fulvio Reggiori, Kathrin Auffarth, Ayelén González Montoro, Bettina Warscheid, Maria Bohnert

Publikováno v: Developmental Cell
Developmental Cell, 45(5), 621-636.e7. CELL PRESS
González Montoro, A, Auffarth, K, Hönscher, C, Bohnert, M, Becker, T, Warscheid, B, Reggiori, F, van der Laan, M, Fröhlich, F & Ungermann, C 2018, ' Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites ', Developmental Cell, vol. 45, no. 5, pp. 621-636.e7 . https://doi.org/10.1016/j.devcel.2018.05.011

The extensive subcellular network of membrane contact sites plays central roles in organelle biogenesis and communication, yet the precise contributions of the involved machineries remain largely enigmatic. The yeast vacuole forms a membrane contact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17b4e1d3bd43918d885926515c7332b9
https://pubmed.ncbi.nlm.nih.gov/29870720