Original Article

TRAPP Stimulates Guanine Nucleotide Exchange on Ypt1p

Correspondence to: Susan Ferro-Novick, Howard Hughes Medical Institute, Yale University School of Medicine, Department of Cell Biology, Boyer Center for Molecular Medicine, 295 Congress Avenue, BCMM 254B, New Haven, CT 06519-1418. Tel:(203) 737-5207 Fax:(203) 737-5746

TRAPP, a novel complex that resides on early Golgi, mediates the targeting of ER-to-Golgi vesicles to the Golgi apparatus. Previous studies have shown that YPT1, which encodes the small GTP-binding protein that regulates membrane traffic at this stage of the secretory pathway, interacts genetically with BET3 and BET5. Bet3p and Bet5p are 2 of the 10 identified subunits of TRAPP. Here we show that TRAPP preferentially binds to the nucleotide-free form of Ypt1p. Mutants with defects in several TRAPP subunits are temperature-sensitive in their ability to displace GDP from Ypt1p. Furthermore, the purified TRAPP complex accelerates nucleotide exchange on Ypt1p. Our findings imply that Ypt1p, which is present on ER-to-Golgi transport vesicles, is activated at the Golgi once it interacts with TRAPP.

Key Words: exchange factor, small GTPase, secretion, ER-to-Golgi, tethering factor

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