期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 45, 页码 32466-32474出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.498329
关键词
Enzyme Mechanisms; Guanine Nucleotide Exchange Factor (GEF); Intracellular Trafficking; Rab Proteins; Small GTPases; Intracellular Trafficking
资金
- German Research Foundation (DFG) Sonderforschungsbereich [SFB1035, B05, SFB642, A4]
- National Natural Science Foundation of China [31200554]
Small G-proteins of the Ras superfamily control the temporal and spatial coordination of intracellular signaling networks by acting as molecular on/off switches. Guanine nucleotide exchange factors (GEFs) regulate the activation of these G-proteins through catalytic replacement of GDP by GTP. During nucleotide exchange, three distinct substrateenzyme complexes occur: a ternary complex with GDP at the start of the reaction (G-proteinGEFGDP), an intermediary nucleotide-free binary complex (G-proteinGEF), and a ternary GTP complex after productive G-protein activation (G-proteinGEFGTP). Here, we show structural snapshots of the full nucleotide exchange reaction sequence together with the G-protein substrates and products using Rabin8/GRAB (GEF) and Rab8 (G-protein) as a model system. Together with a thorough enzymatic characterization, our data provide a detailed view into the mechanism of Rabin8/GRAB-mediated nucleotide exchange.
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