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PLoS One. 2012;7(10):e46386. doi: 10.1371/journal.pone.0046386. Epub 2012 Oct 3.

Sorting signals that mediate traffic of chitin synthase III between the TGN/endosomes and to the plasma membrane in yeast.

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1
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California, USA.

Abstract

Traffic of the integral yeast membrane protein chitin synthase III (Chs3p) from the trans-Golgi network (TGN) to the cell surface and to and from the early endosomes (EE) requires active protein sorting decoded by a number of protein coats. Here we define overlapping signals on Chs3p responsible for sorting in both exocytic and intracellular pathways by the coats exomer and AP-1, respectively. Residues 19DEESLL24, near the N-terminal cytoplasmically-exposed domain, comprise both an exocytic di-acidic signal and an intracellular di-leucine signal. Additionally we show that the AP-3 complex is required for the intracellular retention of Chs3p. Finally, residues R374 and W391, comprise another signal responsible for an exomer-independent alternative pathway that conveys Chs3p to the cell surface. These results establish a role for active protein sorting at the trans-Golgi en route to the plasma membrane (PM) and suggest a possible mechanism to regulate protein trafficking.

PMID:
23056294
PMCID:
PMC3463608
DOI:
10.1371/journal.pone.0046386
[Indexed for MEDLINE]
Free PMC Article
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