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The complex of Arl2‐GTP and PDEδ: from structure to function
Author(s) -
HanzalBayer Michael,
Renault Louis,
Roversi Pietro,
Wittinghofer Alfred,
Hillig Roman C.
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.9.2095
Subject(s) - biology , gtp' , g protein , transport protein , adp ribosylation factor , gtpase , regulator , microbiology and biotechnology , rheb , function (biology) , prenylation , small gtpase , gtp binding protein regulators , effector , vesicular transport proteins , biophysics , biochemistry , signal transduction , n terminus , peptide sequence , endoplasmic reticulum , golgi apparatus , pi3k/akt/mtor pathway , mtorc1 , gene , enzyme
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 PDEδ 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. PDEδ is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H‐Ras, Rheb, Rho6 and Gα i1 interact with PDEδ and that, at least for H‐Ras, the intact C‐terminus is required. We suggest PDEδ to be a specific soluble transport factor for certain prenylated proteins and Arl2‐GTP a regulator of PDEδ‐mediated transport.