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. 2000 Mar 20;148(6):1203–1212. doi: 10.1083/jcb.148.6.1203

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Dependence of CTA1 export on lumenal ER proteins. Microsomes were depleted of their lumenal proteins by extraction with deoxyBigCHAP or were, after extraction, resubstituted with lumenal ER proteins. (a) Mock-treated, extracted, or resubstituted microsomes were loaded with CTA1 by in vitro translation. Export of CTA1 from the different microsomes was analyzed as described in Fig. 3 a. The export rates per hour were 10, 0, and 11% for the mock-treated, extracted, and resubstituted microsomes, respectively. (b) The efficiency of the extraction and resubstitution was verified by the immmunodetection of BiP in equal amounts of mock-treated, extracted, and resubstituted microsomes using an anti-BiP antiserum. (c) Microsomes were reconstituted with CTA1 either in the absence (reconstituted − lumenal proteins) or presence (reconstituted + lumenal proteins) of lumenal ER proteins. Export of CTA1 was analyzed as described in Fig. 3 a, with the exception that CTA1 was detected by immunoblot. The export rates per hour were 0 and 8% in the absence or presence of lumenal proteins, respectively.