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First published online 28 July 2009
doi: 10.1242/jcs.044032

Journal of Cell Science 122, 2924-2934 (2009)
Published by The Company of Biologists 2009
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Research Article

Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER

Helen Hughes1,*, Annika Budnik1,*, Katy Schmidt1,*, Krysten J. Palmer1, Judith Mantell1,3, Chris Noakes1,{ddagger}, Andrew Johnson1,§, Deborah A. Carter3, Paul Verkade1,2,3, Peter Watson1,¶ and David J. Stephens1,**

1 Cell Biology Laboratories, Department of Biochemistry, University of Bristol School of Medical Sciences, University Walk, Bristol BS8 1TD, UK
2 Department of Physiology and Pharmacology, University of Bristol School of Medical Sciences, University Walk, Bristol BS8 1TD, UK
3 Wolfson Bioimaging Facility, University of Bristol School of Medical Sciences, University Walk, Bristol BS8 1TD, UK

** Author for correspondence (david.stephens{at}bristol.ac.uk)

Accepted 18 May 2009

The COPII complex mediates the selective incorporation of secretory cargo and relevant machinery into budding vesicles at specialised sites on the endoplasmic reticulum membrane called transitional ER (tER). Here, we show using confocal microscopy, immunogold labelling of ultrathin cryosections and electron tomography that in human cells at steady state, Sec16 localises to cup-like structures of tER that are spatially distinct from the localisation of other COPII coat components. We show that Sec16 defines the tER, whereas Sec23-Sec24 and Sec13-Sec31 define later structures that precede but are distinct from the intermediate compartment. Steady-state localisation of Sec16 is independent of the localisation of downstream COPII components Sec23-Sec24 and Sec13-Sec31. Sec16 cycles on and off the membrane at a slower rate than other COPII components with a greater immobile fraction. We define the region of Sec16A that dictates its robust localisation of tER membranes and find that this requires both a highly charged region as well as a central domain that shows high sequence identity between species. The central conserved domain of Sec16 binds to Sec13 linking tER membrane localisation with COPII vesicle formation. These data are consistent with a model where Sec16 acts as a platform for COPII assembly at ERES.

Key words: COPII, Membrane traffic, Secretion, Vesicle formation


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Related articles in JCS:

Sec16A: defining an ERES?

JCS 2009 122: 1601. [Full Text]  





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