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The complex of Arl2-GTP and PDEδ: from structure to function

MPS-Authors

Hanzal-Bayer,  Michael
Max Planck Institute of Molecular Physiology, Max Planck Society;

Renault,  Louis
Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98738

Wittinghofer,  Alfred
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

Hillig,  Roman C.
Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Hanzal-Bayer, M., Renault, L., Roversi, P., Wittinghofer, A., & Hillig, R. C. (2002). The complex of Arl2-GTP and PDEδ: from structure to function. EMBO Journal, 21(9): 1, pp. 2095-2106. Retrieved from http://emboj.oupjournals.org/cgi/content/abstract/21/9/2095?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&searchid=1053962082832_2488&stored_search=&FIRSTINDEX=0&volume=21&firstpage=2095&journalcode=emboj.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-0E7C-7
Abstract
Arf-like (Arl) proteins are close relatives of the Arf regulators of vesicular transport, but their function is unknown. Here, we present the crystal structure of full-length Arl2-GTP in complex with its effector PDEdelta solved in two crystal forms (Protein Data Bank codes 1KSG, 1KSH and 1KSJ). Arl2 shows a dramatic conformational change from the GDP-bound form, which suggests that it is reversibly membrane associated. PDEdelta is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H-Ras, Rheb, Rho6 and Galpha(i1) interact with PDEdelta and that, at least for H-Ras, the intact C-terminus is required. We suggest PDEdelta to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDEdelta-mediated transpor