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Published online 28 November 2005. doi:10.1083/jcb.200505145
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 5, 823-833
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Article

 Mutants in trs120 disrupt traffic from the early endosome to the late Golgi

Huaqing Cai1, Yueyi Zhang1, Marc Pypaert2, Lee Walker1, and Susan Ferro-Novick1,2

1 Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06519
2 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06519

Correspondence to Susan Ferro-Novick: susan.ferronovick{at}yale.edu

Transport protein particle (TRAPP), a large complex that mediates membrane traffic, is found in two forms (TRAPPI and -II). Both complexes share seven subunits, whereas three subunits (Trs130p, -120p, and -65p) are specific to TRAPPII. Previous studies have shown that mutations in the TRAPPII-specific gene trs130 block traffic through or from the Golgi. Surprisingly, we report that mutations in trs120 do not block general secretion. Instead, trs120 mutants accumulate aberrant membrane structures that resemble Berkeley bodies and disrupt the traffic of proteins that recycle through the early endosome. Mutants defective in recycling also display a defect in the localization of coat protein I (COPI) subunits, implying that Trs120p may participate in a COPI-dependent trafficking step on the early endosomal pathway. Furthermore, we demonstrate that Trs120p largely colocalizes with the late Golgi marker Sec7p. Our findings imply that Trs120p is required for vesicle traffic from the early endosome to the late Golgi.

Abbreviations used in this paper: Chs3p, chitin synthase III; COP, coat protein; CPY, carboxypeptidase Y; PI[3]P, phosphatidylinositol-3-phosphate; TAP, tandem affinity purification; TRAPP, transport protein particle; vps, vacuolar protein sorting.


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