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
Editorial:
NATL ACAD SCIENCES
Referencias:
Año: 2008 vol. 105 p. 16946 - 16946
Resumen:
ytoplasmic 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