Journal
DEVELOPMENTAL CELL
Volume 2, Issue 3, Pages 283-294Publisher
CELL PRESS
DOI: 10.1016/S1534-5807(02)00127-2
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Funding
- NIGMS NIH HHS [GM26755] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM026755] Funding Source: NIH RePORTER
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In yeast, certain resident trans-Golgi network (TGN) proteins achieve steady-state localization by cycling through late endosomes. Here, we show that chitin synthase III (Chs3p), an enzyme involved in the assembly of the cell wall at the mother-bud junction, populates an intracellular reservoir that is maintained by a cycle of transport between the TGN and early endosomes. Traffic of Chs3p from the TGN/early endosome to the cell surface requires CHS5 and CHS6, mutant alleles of which trap Chs3p in the TGN/early endosome. Disruption of the clathrin adaptor protein complex 1 (AP-1) restores Chs3p transport to the plasma membrane. Similarly, in AP-1 deficient cells, the resident TGN/early endosome syntaxin, TIg1p, is missorted. We propose that clathrin and AP-1 act to recycle Chs3p and TIg1p from the early endosome to the TGN.
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