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The complex of Arl2-GTP and PDE delta: from structure to function
Michael Hanzal-Bayer1, Louis Renault, Pietro Roversi
1Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany.
The EMBO Journal
|May 1, 2002
Summary
Arf-like 2 (Arl2) protein
Area of Science:
- Cellular Biology
- Structural Biology
- Protein Interactions
Background:
- Arf-like (Arl) proteins are related to Arf regulators of vesicular transport, but their functions remain largely unknown.
- Understanding Arl protein function is crucial for elucidating cellular transport mechanisms.
Purpose of the Study:
- To determine the structure of Arl2-GTP in complex with its effector PDE delta.
- To investigate the functional implications of the Arl2-PDE delta interaction and PDE delta's role in protein transport.
Main Methods:
- X-ray crystallography was used to solve the structure of Arl2-GTP/PDE delta complex in two crystal forms.
- Biochemical assays were performed to study the interactions of PDE delta with various prenylated proteins.
Main Results:
- The crystal structure revealed a dramatic conformational change in Arl2 upon GTP binding, suggesting reversible membrane association.
- PDE delta possesses a hydrophobic pocket and interacts with prenylated proteins like H-Ras, Rheb, Rho6, and G alpha(i1).
- The C-terminus of H-Ras is essential for its interaction with PDE delta.
Conclusions:
- PDE delta acts as a specific soluble transport factor for certain prenylated proteins.
- Arl2-GTP likely regulates the transport mediated by PDE delta, contributing to cellular transport pathways.