Sec12 binds to Sec16 at transitional ER sites

COPII vesicles bud from an ER domain known as the transitional ER (tER). Assembly of the COPII coat is initiated by the transmembrane guanine nucleotide exchange factor Sec12. In the budding yeast Pichia pastoris, Sec12 is concentrated at tER sites. Previously, we found that the tER localization of...

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Bibliographic Details
Published in:PloS one 2012-02, Vol.7 (2), p.e31156-e31156
Main Authors: Montegna, Elisabeth A, Bhave, Madhura, Liu, Yang, Bhattacharyya, Dibyendu, Glick, Benjamin S
Format: Article
Language:English
Subjects:
Baking yeast
Binding
Binding Sites
Biology
COP-Coated Vesicles - metabolism
Drug resistance
E coli
Endoplasmic Reticulum - metabolism
Escherichia coli
Exports
Fragmentation
Fungal Proteins - metabolism
Gene expression
Genetics
Guanine
Guanine nucleotide exchange factor
Guanine Nucleotide Exchange Factors - metabolism
Kinases
Localization
Membrane proteins
Membrane Proteins - metabolism
Mutation
Pichia - chemistry
Pichia pastoris
Protein Transport
Proteins
Saccharomyces cerevisiae
Yeast
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Summary:COPII vesicles bud from an ER domain known as the transitional ER (tER). Assembly of the COPII coat is initiated by the transmembrane guanine nucleotide exchange factor Sec12. In the budding yeast Pichia pastoris, Sec12 is concentrated at tER sites. Previously, we found that the tER localization of P. pastoris Sec12 requires a saturable binding partner. We now show that this binding partner is Sec16, a peripheral membrane protein that functions in ER export and tER organization. One line of evidence is that overexpression of Sec12 delocalizes Sec12 to the general ER, but simultaneous overexpression of Sec16 retains overexpressed Sec12 at tER sites. Additionally, when P. pastoris Sec12 is expressed in S. cerevisiae, the exogenous Sec12 localizes to the general ER, but when P. pastoris Sec16 is expressed in the same cells, the exogenous Sec12 is recruited to tER sites. In both of these experimental systems, the ability of Sec16 to recruit Sec12 to tER sites is abolished by deleting a C-terminal fragment of Sec16. Biochemical experiments confirm that this C-terminal fragment of Sec16 binds to the cytosolic domain of Sec12. Similarly, we demonstrate that human Sec12 is concentrated at tER sites, likely due to association with a C-terminal fragment of Sec16A. These results suggest that a Sec12-Sec16 interaction has a conserved role in ER export.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0031156