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          Institute: MPI für molekulare Physiologie     Collection: Sonstige wissenschaftliche Organisationseinheiten     Display Documents

ID: 17930.0, MPI für molekulare Physiologie / Sonstige wissenschaftliche Organisationseinheiten
The complex of Arl2-GTP and PDEδ: from structure to function
Authors:Hanzal-Bayer, Michael; Renault, Louis; Roversi, Pietro; Wittinghofer, Alfred; Hillig, Roman C.
Research Context:vesicular transport
Date of Publication (YYYY-MM-DD):2002-05-01
Title of Journal:EMBO Journal
Journal Abbrev.:Embo J.
Issue / Number:9
Start Page:2095
End Page:2106
Sequence Number of Article:1
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Free Keywords:Arf-like proteins; GDI; phosphodiesterase 6D; Ras; transport
External Publication Status:published
Document Type:Article
Communicated by:Jürgen Block
Affiliations:MPI für molekulare Physiologie/Sonstige Wissenschaftliche Organisationseinheiten/Emeritus-AG: Prof. Dr. Alfred Wittinghofer
External Affiliations:Schering AG, Res Labs, D-13342 Berlin, Germany;
GlobalPhasing Ltd, Cambridge CB3 0AX, England
Identifiers:URL: [abstract of this article with full text links]
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