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. 2001 Jun 11;153(6):1187–1198. doi: 10.1083/jcb.153.6.1187

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© 2001 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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Secretion of immunoreactive insulin is not mediated by a dominant sorting signal in the α-leader. In this case, the α-leader peptide in ICFP has been replaced by a fragment of the HSP150 leader (as described in Materials and Methods). The strains are pep4Δ mutants in order to stabilize the intracellular protein. Cells were pulse labeled for 30 min and chased for 60 min. The lysed cells and media underwent insulin immunoprecipitation before analysis by SDS-PAGE and fluorography.