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Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli.

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The Mon1-Ccz1-Bulli (MCBulli) complex activates Rab7 GTPase, crucial for endosomal and lysosomal functions. Cryo-EM reveals Bulli acts as a scaffold, potentially recruiting other regulators for Rab7 activation.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • The endosomal system is vital for cellular processes, including sorting, recycling, and metabolic signaling.
  • Rab GTPases, particularly Rab7, regulate endosomal maturation, autophagy, and lysosomal function in metazoans.
  • Rab7 activation depends on the Mon1-Ccz1-Bulli (MCBulli) guanine nucleotide exchange factor (GEF) complex.

Purpose of the Study:

  • To elucidate the structural role of the Bulli subunit within the MCBulli complex.
  • To understand the structural basis of Rab7 activation by the MCBulli complex.
  • To compare the MCBulli structure with related complexes involved in cellular trafficking.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structure of the MCBulli complex.
  • Structural analysis focused on the arrangement of Mon1, Ccz1, and Bulli subunits.
  • Comparative structural analysis with homologous complexes was performed.

Main Results:

  • The cryo-EM structure of MCBulli was resolved at 3.2 Å resolution.
  • Bulli was observed as a peripheral, leg-like extension of the Mon1-Ccz1 heterodimer.
  • Structural homology was found with the Fuzzy-Inturned-Wdpcp complex, but with significant differences in subunit interactions.

Conclusions:

  • Bulli's peripheral localization suggests it does not directly participate in the catalytic activation of Rab7.
  • The distinct architecture of MCBulli compared to related complexes indicates divergent functions for Bulli and Wdpcp.
  • Bulli likely functions as a recruitment platform for additional regulators at Rab7 activation sites, influencing endolysosomal trafficking.