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Structural basis of mRNA binding by the human FERRY Rab5 effector complex.

Dennis Quentin1, Jan S Schuhmacher2, Björn U Klink3

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Molecular Cell
|June 2, 2023
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The FERRY complex links mRNA to early endosomes for intracellular distribution. Its unique structure reveals a novel RNA-binding mechanism crucial for mRNA transport and function.

Keywords:
FERRYRab5cryo-EMeffectorendosomesmRNA transportprotein complex

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • The pentameric FERRY complex acts as a molecular link between messenger RNA (mRNA) and early endosomes.
  • This complex plays a crucial role in the intracellular distribution of mRNA.
  • Understanding its structure and function is key to deciphering mRNA transport mechanisms.

Purpose of the Study:

  • To determine the cryo-electron microscopy (cryo-EM) structure of the human FERRY complex.
  • To elucidate the molecular mechanisms underlying FERRY's role in mRNA transport and intracellular distribution.
  • To investigate the functional significance of FERRY's unique architecture and its components.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structural determination of human FERRY.
  • Functional assays to study protein-protein and protein-RNA interactions.
  • Mutational analysis to assess the impact of specific domains on complex assembly and function.

Main Results:

  • The cryo-EM structure revealed a unique, clamp-like architecture for FERRY, distinct from other Rab effectors.
  • The Fy-2 subunit acts as a central hub, connecting other subunits (Fy-1/3, Fy-5) and mediating binding to Rab5 and mRNA.
  • Both coiled-coil domains and the Fy-5 component are involved in mRNA binding, indicating a novel RNA-binding mode.

Conclusions:

  • The FERRY complex possesses a unique architecture enabling a previously undescribed mode of RNA binding via coiled-coil domains.
  • The Fy-2 subunit is essential for FERRY complex assembly, Rab5 binding, and mRNA interaction, highlighting its role as a binding hub.
  • This study provides critical mechanistic insights into long-distance mRNA transport and its regulation by the FERRY complex.