Myo1c binding to submembrane actin mediates insulin-induced tethering of GLUT4 vesicles
Author
dc.contributor.author
Boguslavsky, Shlomit
Author
dc.contributor.author
Chiu, Tim
Author
dc.contributor.author
Foley, Kevin P.
Author
dc.contributor.author
Osorio-Fuentealba, Cesar
Author
dc.contributor.author
Antonescu, Costin N.
Author
dc.contributor.author
Bayer, K. Ulrich
Author
dc.contributor.author
Bilan, Philip J.
Author
dc.contributor.author
Klip, Amira
Admission date
dc.date.accessioned
2018-12-20T14:13:58Z
Available date
dc.date.available
2018-12-20T14:13:58Z
Publication date
dc.date.issued
2012
Cita de ítem
dc.identifier.citation
Molecular Biology of the Cell, Volumen 23, Issue 20, 2018, Pages 4065-4078
Identifier
dc.identifier.issn
10591524
Identifier
dc.identifier.issn
19394586
Identifier
dc.identifier.other
10.1091/mbc.E12-04-0263
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/155045
Abstract
dc.description.abstract
GLUT4-containing vesicles cycle between the plasma membrane and intracellular compartments. Insulin promotes GLUT4 exocytosis by regulating GLUT4 vesicle arrival at the cell periphery and its subsequent tethering, docking, and fusion with the plasma membrane. The molecular machinery involved in GLUT4 vesicle tethering is unknown. We show here that Myo1c, an actin-based motor protein that associates with membranes and actin filaments, is required for insulin-induced vesicle tethering in muscle cells. Myo1c was found to associate with both mobile and tethered GLUT4 vesicles and to be required for vesicle capture in the total internal reflection fluorescence (TIRF) zone beneath the plasma membrane. Myo1c knockdown or overexpression of an actin binding-deficient Myo1c mutant abolished insulin-induced vesicle immobilization, increased GLUT4 vesicle velocity in the TIRF zone, and prevented their externalization. Conversely, Myo1c overexpression immobilized GLUT4 vesicles in the TIRF zone and