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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Autores principales:	Elisabeth A Montegna, Madhura Bhave, Yang Liu, Dibyendu Bhattacharyya, Benjamin S Glick
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fb27a57e113b480ab4858a900d45f22f
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spelling	oai:doaj.org-article:fb27a57e113b480ab4858a900d45f22f2021-11-18T07:28:39ZSec12 binds to Sec16 at transitional ER sites.1932-620310.1371/journal.pone.0031156https://doaj.org/article/fb27a57e113b480ab4858a900d45f22f2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22347445/?tool=EBIhttps://doaj.org/toc/1932-6203COPII 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.Elisabeth A MontegnaMadhura BhaveYang LiuDibyendu BhattacharyyaBenjamin S GlickPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e31156 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Elisabeth A Montegna Madhura Bhave Yang Liu Dibyendu Bhattacharyya Benjamin S Glick Sec12 binds to Sec16 at transitional ER sites.
description	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.
format	article
author	Elisabeth A Montegna Madhura Bhave Yang Liu Dibyendu Bhattacharyya Benjamin S Glick
author_facet	Elisabeth A Montegna Madhura Bhave Yang Liu Dibyendu Bhattacharyya Benjamin S Glick
author_sort	Elisabeth A Montegna
title	Sec12 binds to Sec16 at transitional ER sites.
title_short	Sec12 binds to Sec16 at transitional ER sites.
title_full	Sec12 binds to Sec16 at transitional ER sites.
title_fullStr	Sec12 binds to Sec16 at transitional ER sites.
title_full_unstemmed	Sec12 binds to Sec16 at transitional ER sites.
title_sort	sec12 binds to sec16 at transitional er sites.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fb27a57e113b480ab4858a900d45f22f
work_keys_str_mv	AT elisabethamontegna sec12bindstosec16attransitionalersites AT madhurabhave sec12bindstosec16attransitionalersites AT yangliu sec12bindstosec16attransitionalersites AT dibyendubhattacharyya sec12bindstosec16attransitionalersites AT benjaminsglick sec12bindstosec16attransitionalersites
_version_	1718423449389498368

Sec12 binds to Sec16 at transitional ER sites.

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