English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15

Hirst, J., Borner, G. H. H., Edgar, J., Hein, M. Y., Mann, M., Buchholz, F., et al. (2013). Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. MOLECULAR BIOLOGY OF THE CELL, 24(16), 2558-2569. doi:10.1091/mbc.E13-03-0170.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Hirst, Jennifer1, Author
Borner, Georg H. H.1, Author
Edgar, James1, Author
Hein, Marco Y.2, Author              
Mann, Matthias2, Author              
Buchholz, Frank1, Author
Antrobus, Robin1, Author
Robinson, Margaret S.1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

Content

show
hide
Free keywords: MOLECULAR ARCHITECTURE; STRUCTURE PREDICTION; COMPLEXES; QUANTIFICATION; IDENTIFICATION; SPATACSIN; SIGNALS; SERVER; GENE; AP2
 Abstract: The AP-5 complex is a recently identified but evolutionarily ancient member of the family of heterotetrameric adaptor proteins (AP complexes). It is associated with two proteins that are mutated in patients with hereditary spastic paraplegia, SPG11 and SPG15. Here we show that the four AP-5 subunits can be coimmunoprecipitated with SPG11 and SPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of similar to 1:1:1:1:1:1. Knockdowns of SPG11 or SPG15 phenocopy knockdowns of AP-5 subunits:all six knockdowns cause the cation-independent mannose 6-phosphate receptor to become trapped in clusters of early endosomes. In addition, AP-5, SPG11, and SPG15 colocalize on a late endosomal/lysosomal compartment. Both SPG11 and SPG15 have predicted secondary structures containing alpha-solenoids related to those of clathrin heavy chain and COPI subunits. SPG11 also has an N-terminal, beta-propeller-like domain, which interacts in vitro with AP-5. We propose that AP-5, SPG15, and SPG11 form a coat-like complex, with AP-5 involved in protein sorting, SPG15 facilitating the docking of the coat onto membranes by interacting with PI3P via its FYVE domain, and SPG11 (possibly together with SPG15) forming a scaffold.

Details

show
hide
Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000324492900007
DOI: 10.1091/mbc.E13-03-0170
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: MOLECULAR BIOLOGY OF THE CELL
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA : AMER SOC CELL BIOLOGY
Pages: - Volume / Issue: 24 (16) Sequence Number: - Start / End Page: 2558 - 2569 Identifier: ISSN: 1059-1524