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Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum

Wendeler, M. W. and Paccaud, J. -P. and Hauri, H. -P.. (2007) Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO reports, Vol. 8, H. 3. pp. 258-264.

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Official URL: http://edoc.unibas.ch/dok/A5257742

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Abstract

Sec24 of the COPII (coat protein complex II) vesicle coat mediates the selective export of membrane proteins from the endoplasmic reticulum (ER) in yeast. Human cells express four Sec24 isoforms, but their role is unknown. Here, we report the differential effects of Sec24 isoform-specific silencing on the transport of the membrane reporter protein ERGIC-53 (ER-Golgi intermediate compartment-53) carrying the cytosolic ER export signals di-phenylalanine, di-tyrosine, di-leucine, di-isoleucine, di-valine or terminal valine. Knockdown of single Sec24 isoforms showed dependence of di-leucine-mediated transport on Sec24A, but transport mediated by the other signals was not affected. By contrast, double knockdown of Sec24A with one of the other three Sec24 isoforms impaired all aromatic/hydrophobic signal-dependent transport. Double knockdown of Sec24B/C or Sec24B/D preferentially affected di-leucine-mediated transport, whereas knockdown of Sec24C/D affected di-isoleucine- and valine-mediated transport. The isoform-selective transport correlated with binding preferences of the signals for the corresponding isoforms in vitro. Thus, human Sec24 isoforms expand the repertoire of cargo for signal-mediated ER export, but are in part functionally redundant.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri)
UniBasel Contributors:Hauri, Hans-Peter
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:1469-221X
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:18

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