The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes.

Small Rab GTPases are involved in the regulation of membrane trafficking. They cycle between cytosolic and membrane-bound forms. These membrane association/dissociation are tightly controlled by regulatory proteins. To search for proteins interacting with Rab13, a small GTPase associated with vesicles in fibroblasts and predominantly with tight junctions in epithelial cells, ...
we screened a HeLa two-hybrid cDNA library and isolated a clone encoding a protein of 17.4 kDa. This protein, almost identical to the bovine rod cGMP phosphodiesterase delta subunit, was named human delta-PDE. The delta-PDE binds specifically to Rab13. It exhibits two putative C-terminal sequences necessary for the interaction with PDZ (PSD95, Dlg, ZO-1) domains contained in many proteins localized to specific plasma membrane microdomains. Immunofluorescence microscopic studies revealed that the vesicular stomatitis virus (VSV)-tagged delta-PDE is localized in vesicular structures accumulated near the plasma membrane in epithelial cells. Deletion of the PDZ binding motifs impair VSV-delta-PDE subcellular distribution. Purified recombinant delta-PDE had the capacity to dissociate Rab13 from cellular membranes. Our data support the proposal that delta-PDE, but not GDP dissociation inhibitor, may serve to control the dynamic of the association of Rab13 with cellular membranes.
Mesh Terms:
3',5'-Cyclic-GMP Phosphodiesterases, Amino Acid Sequence, Animals, Cattle, Cell Membrane, GTP Phosphohydrolases, GTP-Binding Proteins, Hela Cells, Humans, LLC-PK1 Cells, Membrane Glycoproteins, Microscopy, Fluorescence, Molecular Sequence Data, Retinal Rod Photoreceptor Cells, Sequence Homology, Amino Acid, Subcellular Fractions, Swine, Viral Envelope Proteins, rab GTP-Binding Proteins
J. Biol. Chem.
Date: Aug. 28, 1998
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