Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1–Ccz1

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Titel: Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1–Ccz1
Autor(en): Kiontke, Stephan
Langemeyer, Lars
Kuhlee, Anne
Schuback, Saskia
Raunser, Stefan
Ungermann, Christian
Kümmel, Daniel
Zusammenfassung: The Mon1–Ccz1 complex (MC1) is the guanine nucleotide exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 and is required for endosomal maturation and fusion at the vacuole/ lysosome. Here we present the overall architecture of MC1 from Chaetomium thermophilum , and in combining biochemical studies and mutational analysis in yeast, we identify the domains required for catalytic activity, complex assembly and localization of MC1. The crystal structure of a catalytic MC1 core complex bound to Ypt7 provides mechanistic insight into its function. We pinpoint the determinants that allow for a discrimination of the Rab7-like Ypt7 over the Rab5-like Vps21, which are both located on the same membrane. MC1 shares structural similarities with the TRAPP complex, but employs a novel mechanism to promote nucleotide exchange that utilizes a conserved lysine residue of Ypt7, which is inserted upon MC1 binding into the nucleotide-binding pocket of Ypt7 and contributes to specificity.
Bibliografische Angaben: Nature Communications 8, Article number: 14034, 2017
URL: https://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018043016920
Schlagworte: Endosome; MC1; Guanine nucleotide exchange factor; Rab GTPase; Ypt7; Rab7
Erscheinungsdatum: 30-Apr-2018
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