CHC22 clathrin mediates traffic from early secretory compartments for human GLUT4 pathway biogenesis - Sorbonne Université
Journal Articles Journal of Cell Biology Year : 2020

CHC22 clathrin mediates traffic from early secretory compartments for human GLUT4 pathway biogenesis

Abstract

Glucose transporter 4 (GLUT4) is sequestered inside muscle and fat and then released by vesicle traffic to the cell surface in response to postprandial insulin for blood glucose clearance. Here, we map the biogenesis of this GLUT4 traffic pathway in humans, which involves clathrin isoform CHC22. We observe that GLUT4 transits through the early secretory pathway more slowly than the constitutively secreted GLUT1 transporter and localize CHC22 to the ER-to-Golgi intermediate compartment (ERGIC). CHC22 functions in transport from the ERGIC, as demonstrated by an essential role in forming the replication vacuole of Legionella pneumophila bacteria, which requires ERGIC-derived membrane. CHC22 complexes with ERGIC tether p115, GLUT4, and sortilin, and downregulation of either p115 or CHC22, but not GM130 or sortilin, abrogates insulin-responsive GLUT4 release. This indicates that CHC22 traffic initiates human GLUT4 sequestration from the ERGIC and defines a role for CHC22 in addition to retrograde sorting of GLUT4 after endocytic recapture, enhancing pathways for GLUT4 sequestration in humans relative to mice, which lack CHC22.
Fichier principal
Vignette du fichier
jcb_201812135.pdf (5.33 Mo) Télécharger le fichier
Origin Publication funded by an institution
Loading...

Dates and versions

hal-02555498 , version 1 (27-04-2020)

Identifiers

Cite

Stéphane M Camus, Marine Camus, Carmen Figueras-Novoa, Gaelle Boncompain, L. Amanda Sadacca, et al.. CHC22 clathrin mediates traffic from early secretory compartments for human GLUT4 pathway biogenesis. Journal of Cell Biology, 2020, 219 (1), ⟨10.1083/jcb.201812135⟩. ⟨hal-02555498⟩
96 View
56 Download

Altmetric

Share

More