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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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Model of ICFP and insulin sorting in the secretory pathway of yeast cells. According to this schema, ICFP is quantitatively delivered to the Golgi complex where it may encounter Kex2p. To the extent that the precursor protein is unprocessed by Kex2p, it is delivered to the cell surface via the secretory pathway. To the extent that ICFP is endoproteolytically processed in the Golgi complex, insulin is retained intracellularly and is delivered ultimately to the vacuole. Note that the α-leader peptide contains no [³⁵S]cysteine residues; thus, we have not analyzed the fate of the α-leader peptide after cleavage from the insulin moiety.