TY - JOUR
T1 - Traffic of p24 proteins and COPII coat composition mutually influence membrane scaffolding
AU - D'Arcangelo, Jennifer G.
AU - Crissman, Jonathan
AU - Pagant, Silvere
AU - Čopič, Alenka
AU - Latham, Catherine F.
AU - Snapp, Erik L.
AU - Miller, Elizabeth A.
N1 - Funding Information:
We thank Charlie Barlowe, Manuel Muniz, and Randy Schekman for providing strains and plasmids. Research reported in this publication was supported by NIGMS of the NIH under award number R01GM085089 (E.A.M.) and by a Columbia Research Initiatives in Science and Engineering award (E.A.M.). J.G.D. was supported by an NIH institutional research training grant (T32GM008798). A.Č. was supported by a Columbia Frontiers of Science fellowship. E.L.S. is supported by a grant to the Marion Bessin Liver Center (NIH/NIDDK 5P30 DK041296) and is grateful for the use of microscopes in the Albert Einstein College of Medicine Analytical Imaging Facility and the resources of the Cell Structure and Imaging Core of the Marion Bessin Liver Center.
Publisher Copyright:
© 2015 Elsevier Ltd.
PY - 2015/5/18
Y1 - 2015/5/18
N2 - Eukaryotic protein secretion requires efficient and accurate delivery of diverse secretory and membrane proteins. This process initiates in the ER, where vesicles are sculpted by the essential COPII coat. The Sec13p subunit of the COPII coat contributes to membrane scaffolding, which enforces curvature on the nascent vesicle. A requirement for Sec13p can be bypassed when traffic of lumenally oriented membrane proteins is abrogated. Here we sought to further explore the impact of cargo proteins on vesicle formation. We show that efficient ER export of the p24 family of proteins is a major driver of the requirement for Sec13p. The scaffolding burden presented by the p24 complex is met in part by the cargo adaptor Lst1p, which binds to a subset of cargo, including the p24 proteins. We propose that the scaffolding function of Lst1p is required to generate vesicles that can accommodate difficult cargo proteins that include large oligomeric assemblies and asymmetrically distributed membrane proteins. Vesicles that contain such cargoes are also more dependent on scaffolding by Sec13p, and may serve as a model for large carrier formation in other systems.
AB - Eukaryotic protein secretion requires efficient and accurate delivery of diverse secretory and membrane proteins. This process initiates in the ER, where vesicles are sculpted by the essential COPII coat. The Sec13p subunit of the COPII coat contributes to membrane scaffolding, which enforces curvature on the nascent vesicle. A requirement for Sec13p can be bypassed when traffic of lumenally oriented membrane proteins is abrogated. Here we sought to further explore the impact of cargo proteins on vesicle formation. We show that efficient ER export of the p24 family of proteins is a major driver of the requirement for Sec13p. The scaffolding burden presented by the p24 complex is met in part by the cargo adaptor Lst1p, which binds to a subset of cargo, including the p24 proteins. We propose that the scaffolding function of Lst1p is required to generate vesicles that can accommodate difficult cargo proteins that include large oligomeric assemblies and asymmetrically distributed membrane proteins. Vesicles that contain such cargoes are also more dependent on scaffolding by Sec13p, and may serve as a model for large carrier formation in other systems.
UR - http://www.scopus.com/inward/record.url?scp=84929607301&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84929607301&partnerID=8YFLogxK
U2 - 10.1016/j.cub.2015.03.029
DO - 10.1016/j.cub.2015.03.029
M3 - Article
AN - SCOPUS:84929607301
SN - 0960-9822
VL - 25
SP - 1296
EP - 1305
JO - Current Biology
JF - Current Biology
IS - 10
ER -