English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Mechanistic insights into the role of prenyl-binding protein PrBP/delta in membrane dissociation of phosphodiesterase 6

Qureshi, B. M., Schmidt, A., Behrmann, E., Buerger, J., Mielke, T., Spahn, C. M. T., et al. (2018). Mechanistic insights into the role of prenyl-binding protein PrBP/delta in membrane dissociation of phosphodiesterase 6. Nature Communications, 9: 90. doi:10.1038/s41467-017-02569-y.

Item is

Basic

show hide
Genre: Journal Article
Other : Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6

Files

show Files
hide Files
:
s41467-017-02569-y.pdf (Publisher version), 4MB
Name:
s41467-017-02569-y.pdf
Description:
Open Access fulltext
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
+ fulltext / Open Access
OA-Status:

Creators

show
hide
 Creators:
Qureshi, Bilal M.1, Author
Schmidt, Andrea1, Author
Behrmann, Elmar2, Author           
Buerger, Joerg1, Author
Mielke, Thorsten1, Author
Spahn, Christian M. T.1, Author
Heck, Martin1, Author
Scheerer, Patrick1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Max Planck Research Group Structural Dynamics of Proteins, Center of Advanced European Studies and Research (caesar), Max Planck Society, Ludwig-Erhard-Allee 2, 53175 Bonn, DE, ou_2173687              

Content

show
hide
Free keywords: -
 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/δ), at 1.81 Å resolution in its ligand-free apo-form. Apo-PrBP/δ harbors a preshaped, deep hydrophobic cavity, capacitating apo-PrBP/δ to readily bind its prenylated cargo. To investigate the molecular mechanism of cargo solubilization we analyzed the PrBP/δ-induced membrane dissociation of rod photoreceptor phosphodiesterase (PDE6). The results suggest that PrBP/δ 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/δ 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/δ.

Details

show
hide
Language(s): eng - English
 Dates: 2018-01-082018-12-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000419446600018
DOI: 10.1038/s41467-017-02569-y
PMID: 29311697
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
  Abbreviation : Nat Commun
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 9 Sequence Number: 90 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723