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TitleCryo-EM structure of the human MON1A-CCZ1-RAB7A complex provides insights into nucleotide exchange mechanism.
Journal, issue, pagesLife Metab, Vol. 4, Issue 5, Page loaf017, Year 2025
Publish dateMay 26, 2025
AuthorsXinna Li / Dan Li / Dan Tang / Xiaofang Huang / Hui Bao / Jiawei Wang / Shiqian Qi /
PubMed AbstractAutophagy is a fundamental cellular process, conserved across species from yeast to mammals, that plays a crucial role in maintaining cellular homeostasis. The functionally conserved MON1-CCZ1 (MC1) ...Autophagy is a fundamental cellular process, conserved across species from yeast to mammals, that plays a crucial role in maintaining cellular homeostasis. The functionally conserved MON1-CCZ1 (MC1) complex serves as a guanine nucleotide exchange factor (GEF) for the RAB GTPase RAB7A and is indispensable for directing RAB7A recruitment to autophagosome or lysosomal membranes. Despite its critical role, the precise molecular mechanism underlying the assembly of the human MON1A-CCZ1 (HsMC1) complex and its specific GEF activity towards RAB7A has remained unclear. In this study, we report the high-resolution cryo-electron microscopy (cryo-EM) structure of the HsMC1 GEF domain in a complex with the nucleotide-free RAB7A at 2.85 Å resolution. Our structural data demonstrate that engagement with the HsMC1 complex induces marked conformational shifts in the phosphate-binding loop (P-loop) and Switch I/II regions of RAB7A. A striking feature of this complex is the direct interaction between the P-loop of RAB7A and CCZ1, a structural detail not previously observed. Furthermore, biochemical assays targeting residues within Interface I or II of the HsMC1-RAB7A complex highlight their critical role in mediating the interaction and suggest a unique mechanism for nucleotide exchange facilitated by the HsMC1 complex. These findings provide novel molecular insights into the functional mechanisms of the HsMC1-RAB7A complex, offering a robust structural framework to inform future investigations into disease-related targets and therapeutic development.
External linksLife Metab / PubMed:40979223 / PubMed Central
MethodsEM (single particle)
Resolution2.85 Å
Structure data

63249

9lol

EMDB-63249, PDB-9lol:
Cryo-EM structure of human MON1A-CCZ1-RAB7A
Method: EM (single particle) / Resolution: 2.85 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / Complex / GEF / RAB-GTPase

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