Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1995 Dec 29;270(52):31364-71.

In vitro assembly and disassembly of coatomer.

Author information

  • 1Département de Biologie Cellulaire, Université de Genève, Sciences III, Geneva, Switzerland.

Abstract

Coatomer, a complex of seven proteins, is the major component of the non-clathrin (COP I) membrane coat. We report here the first system to reversibly disassemble and reassemble this complex in vitro. Coatomer disassembles at high salt concentrations and reassembles when returned to a more physiological buffer. Using this system, we show that alpha-, beta'-, and epsilon-COP interact directly and that gamma-COP interacts with zeta-COP. A partial complex comprising alpha-, beta'-, and epsilon-COP, obtained after coatomer disassembly, can bind to membranes in vitro. This binding is, at least in part, mediated by interactions with cytoplasmic KKXX motifs of proteins normally retained in or retrieved to the endoplasmic reticulum. Using coatomer disassembly and epitope-specific antibodies, we also demonstrate that the N- and C-terminal domains of beta-COP are buried within the native coatomer complex. These results provide the first insights into how the coatomer is structured.

PMID:
8537409
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

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