Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
EMBO J. 2007 Nov 14;26(22):4788-800. Epub 2007 Oct 18.

The PX-BAR membrane-remodeling unit of sorting nexin 9.

Author information

  • 1Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology, Dortmund, Germany.

Abstract

Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism.

PMID:
17948057
[PubMed - indexed for MEDLINE]
PMCID:
PMC2080800
Free PMC Article

Images from this publication.See all images (6)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk