INVESTIGADORES
AMBROGGIO Ernesto Esteban
artículos
Título:
COPI coat assembly occurs on liquid-disordered domains and the associated membrane deformations are limited by membrane tension
Autor/es:
JEAN-BAPTISTE MANNEVILLE; JEAN-FRANÇOIS CASELLA; ERNESTO AMBROGGIO; PIERRE GOUNON; JULIEN BERTHERAT; PATRICIA BASSEREAU; JEAN CARTAUD; BRUNO ANTONNY; BRUNO GOUD
Revista:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Editorial:
NATL ACAD SCIENCES
Referencias:
Año: 2008 vol. 105 p. 16946 - 16951
ISSN:
0027-8424
Resumen:
Cytoplasmic coat proteins are required for cargo selection and budding
of tubulovesicular transport intermediates that shuttle
between intracellular compartments. To better
understand the physical parameters governing coat assembly and
coat-induced
membrane deformation, we have reconstituted the
Arf1-dependent assembly of the COPI coat on giant unilamellar vesicles
by
using fluorescently labeled Arf1 and coatomer.
Membrane recruitment of Arf1-GTP occurs exclusively on disordered lipid
domains
and does not induce optically visible membrane
deformation. In the presence of Arf1-GTP, coatomer self-assembles into
weakly
curved coats on membranes under high tension, while
it induces extensive membrane deformation at low membrane tension.
These
deformations appear to have a composition different
from the parental membrane because they are protected from phase
transition.
These findings suggest that the COPI coat is
adapted to liquid disordered membrane domains where it could promote
lipid sorting
and that its mechanical effects can be tuned by
membrane tension.