Qureshi, Bilal M., Schmidt, Andrea, Behrmann, Elmar ORCID: 0000-0001-6794-3669, Buerger, Joerg, Mielke, Thorsten, Spahn, Christian M. T., Heck, Martin and Scheerer, Patrick ORCID: 0000-0001-5028-2075 (2018). Mechanistic insights into the role of prenyl-binding protein PrBP/delta in membrane dissociation of phosphodiesterase 6. Nat. Commun., 9. LONDON: NATURE PUBLISHING GROUP. ISSN 2041-1723
Full text not available from this repository.Abstract
Isoprenylated proteins are associated with membranes and their inter-compartmental distribution is regulated by solubilization factors, which incorporate lipid moieties in hydrophobic cavities and thereby facilitate free diffusion during trafficking. Here we report the crystal structure of a solubilization factor, the prenyl-binding protein (PrBP/delta), at 1.81 angstrom resolution in its ligand-free apo-form. Apo-PrBP/delta harbors a preshaped, deep hydrophobic cavity, capacitating apo-PrBP/delta to readily bind its prenylated cargo. To investigate the molecular mechanism of cargo solubilization we analyzed the PrBP/delta-induced membrane dissociation of rod photoreceptor phosphodiesterase (PDE6). The results suggest that PrBP/delta exclusively interacts with the soluble fraction of PDE6. Depletion of soluble species in turn leads to dissociation of membrane-bound PDE6, as both are in equilibrium. This solubilization by depletion mechanism of PrBP/delta differs from the extraction of prenylated proteins by the similar folded solubilization factor RhoGDI, which interacts with membrane bound cargo via an N-terminal structural element lacking in PrBP/delta.
Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||
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URN: | urn:nbn:de:hbz:38-199052 | ||||||||||||||||||||||||||||||||||||
DOI: | 10.1038/s41467-017-02569-y | ||||||||||||||||||||||||||||||||||||
Journal or Publication Title: | Nat. Commun. | ||||||||||||||||||||||||||||||||||||
Volume: | 9 | ||||||||||||||||||||||||||||||||||||
Date: | 2018 | ||||||||||||||||||||||||||||||||||||
Publisher: | NATURE PUBLISHING GROUP | ||||||||||||||||||||||||||||||||||||
Place of Publication: | LONDON | ||||||||||||||||||||||||||||||||||||
ISSN: | 2041-1723 | ||||||||||||||||||||||||||||||||||||
Language: | English | ||||||||||||||||||||||||||||||||||||
Faculty: | Faculty of Mathematics and Natural Sciences | ||||||||||||||||||||||||||||||||||||
Divisions: | Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry | ||||||||||||||||||||||||||||||||||||
Subjects: | no entry | ||||||||||||||||||||||||||||||||||||
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Refereed: | Yes | ||||||||||||||||||||||||||||||||||||
URI: | http://kups.ub.uni-koeln.de/id/eprint/19905 |
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