TRAPP stimulates guanine nucleotide exchange on Ypt1p

Journal of Cell Biology

Volumn 151, Issue 2, 2000, Pages 289-295

  Wang, Wei ^a   Sacher, Michael ^a   Ferro Novick, Susan ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

ER to Golgi; Exchange factor; Secretion; Small GTPase; Tethering factor

Indexed keywords

GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE;

ARTICLE; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; GOLGI COMPLEX; MEMBRANE VESICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN TRANSPORT; YEAST CELL;

CARRIER PROTEINS; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; GOLGI APPARATUS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; GUANINE NUCLEOTIDES; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MEMBRANE PROTEINS; PROTEIN TRANSPORT; RAB GTP-BINDING PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSPORT VESICLES; VESICULAR TRANSPORT PROTEINS;

EID: 0034676094     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.151.2.289     Document Type: Article

References (31)

1. The GTP-binding protein Ypt1 is required for transport in vitro: The Golgi apparatus is defective in ypt1 mutants
2. Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
3. TRAPP stably associates with the Golgi and is required for vesicle docking
4. Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast
5. Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes
6. Identification and structure of four yeast genes (SLY1) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily
7. Identification of a Sec4p GTPase-activating protein (GAP) as a novel member of a Rab GAP family
8. Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport
9. VPS21 encodes a rab5-like GTP binding protein that is required for the sorting of yeast vacuolar proteins
10. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
11. Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
12. A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport
13. Requirement of nucleotide exchange for Ypt1p GTPase mediated protein transport
14. Identification of regulators for Ypt1p GTPase nucleotide cycling
15. Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic
16. High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking
17. Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins
18. Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence
19. Rab proteins
20. The diversity of Rab proteins in vesicle transport
21. Viral harvey ras p21 expressed in Escherichia coli purifies as a binary one-to-one complex with GDP
22. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs
23. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion
24. Identification and characterization of five new subunits of TRAPP
25. A ras-like protein is required for a post-Golgi event in yeast secretion
26. GTPase-activating proteins: Helping hands to complement an active site
27. Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1p protein
28. The yeast GTP-binding Ypt1 protein and a mammalian counterpart are associated with the secretion machinery
29. Role of three rab5-like GTPases, Ypt51p, Ypt52p, and Ypt53p, in the endocytic and vacuolar protein sorting pathways of yeast
30. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p
31. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles