Proteomic analysis of adaptor protein 1A coats selectively assembled on liposomes.

Abstract:

:Coat components localize to specific membrane domains, where they sort selected transmembrane proteins. To study how clathrin coats are stabilized on such domains and to identify the protein networks involved, we combined proteomic screens and in vitro liposome-based assays that recapitulate the fidelity of protein sorting in vivo. Our study identifying approximately 40 proteins on AP-1A-coated liposomes revealed that AP-1A coat assembly triggers the concomitant recruitment of Rac1, its effectors, and the Wave/Scar complex as well as that of Rab11 and Rab14. The coordinated recruitment of these different machineries requires a mosaic of membrane components comprising the GTPase ADP-ribosylation factor 1, sorting signals in selected transmembrane proteins, and phosphatidylinositol 4-phosphate. These results demonstrate that the combinatorial use of low-affinity binding sites present on the same membrane domain accounts not only for a selective coat assembly but also for the coordinated assembly of selected machineries required for actin polymerization and subsequent membrane fusion.

authors

Baust T,Czupalla C,Krause E,Bourel-Bonnet L,Hoflack B

doi

10.1073/pnas.0511062103

keywords:

subject

Has Abstract

pub_date

2006-02-28 00:00:00

pages

3159-64

issue

9

eissn

0027-8424

issn

1091-6490

pii

0511062103

journal_volume

103

pub_type

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