The Sec34/35 Golgi Transport Complex Is Related to the Exocyst, Defining a Family of Complexes Involved in Multiple Steps of Membrane Traffic

• Published in: Developmental cell 2001-10, Vol.1 (4), p.527-537
• Main Authors: Whyte, James R.C., Munro, Sean
• Format: Article
• Language: English
• Subjects: Adaptor Proteins, Vesicular Transport; Animals; Carrier Proteins - metabolism; COS Cells; Dor1 protein; exocyst; Fungal Proteins - genetics; Fungal Proteins - metabolism; Golgi Apparatus - metabolism; Humans; Membrane Proteins - genetics; Membrane Proteins - metabolism; membrane trafficking; Molecular Sequence Data; Mutation - physiology; Phenotype; Protein Transport - physiology; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sec34 protein; Sec35 protein; Sequence Homology, Amino Acid; Vesicular Transport Proteins; Yeasts
• ISSN: 1534-5807; 1878-1551
• DOI: 10.1016/S1534-5807(01)00063-6

The specificity of intracellular vesicle transport is mediated in part by tethering factors that attach the vesicle to the destination organelle prior to fusion. We have identified a protein, Dor1p, that is involved in vesicle targeting to the yeast Golgi apparatus and found it to be associated with seven further proteins. Identification of these revealed that they include Sec34p and Sec35p, the two known components of the Sec34/35 complex previously proposed to tether vesicles to the Golgi. Of the six previously uncharacterized components, four have homologs in higher eukaryotes, including a subunit of a mammalian Golgi transport complex. Furthermore, several of the proteins show distant homology to components of two other putative tethering complexes, the exocyst and the Vps52/53/54 complex, revealing that tethering factors involved in different membrane traffic steps are structurally related.