DOI: 10.1083/jcb.200104093. The Tlg SNARE complex is required for TGN homotypic fusion

The Tlg SNARE complex is required for TGN homotypic fusion

10.1083/jcb.200104093

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

Using a new assay for membrane fusion between late Golgi/endosomal compartments, we have reconstituted a rapid, robust homotypic fusion reaction between membranes containing Kex2p and Ste13p, two enzymes resident in the yeast trans-Golgi network (TGN). Fusion was temperature, ATP, and cytosol dependent. It was inhibited by dilution, Ca+2 chelation, N-ethylmaleimide, and detergent. Coimmunoisolation confirmed that the reaction resulted in cointegration of the two enzymes into the same bilayer. Antibody inhibition experiments coupled with antigen competition indicated a requirement for soluble NSF attachment protein receptor (SNARE) proteins Tlg1p, Tlg2p, and Vti1p in this reaction. Membrane fusion also required the rab protein Vps21p. Vps21p was sufficient if present on either the Kex2p or Ste13p membranes alone, indicative of an inherent symmetry in the reaction. These results identify roles for a Tlg SNARE complex composed of Tlg1p, Tlg2p, Vti1p, and the rab Vps21p in this previously uncharacterized homotypic TGN fusion reaction.

Authors 4

Jason H. Brickner (first)
Jennifer M. Blanchette (additional)
György Sipos (additional)
Robert S. Fuller (additional)

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Dates

Type	When
Created	23 years ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 22, 2023, 9:14 a.m.)
Indexed	1 year, 10 months ago (Oct. 2, 2023, 6:28 a.m.)
Issued	23 years, 8 months ago (Dec. 10, 2001)
Published	23 years, 8 months ago (Dec. 10, 2001)
Published Online	23 years, 8 months ago (Dec. 10, 2001)
Published Print	23 years, 8 months ago (Dec. 10, 2001)

Funders 0

None

BibTeX

@article{Brickner_2001, title={The Tlg SNARE complex is required for TGN homotypic fusion}, volume={155}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200104093}, DOI={10.1083/jcb.200104093}, number={6}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Brickner, Jason H. and Blanchette, Jennifer M. and Sipos, György and Fuller, Robert S.}, year={2001}, month=dec, pages={969–978} }

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  "abstract": "<jats:p>Using a new assay for membrane fusion between late Golgi/endosomal compartments, we have reconstituted a rapid, robust homotypic fusion reaction between membranes containing Kex2p and Ste13p, two enzymes resident in the yeast trans-Golgi network (TGN). Fusion was temperature, ATP, and cytosol dependent. It was inhibited by dilution, Ca+2 chelation, N-ethylmaleimide, and detergent. Coimmunoisolation confirmed that the reaction resulted in cointegration of the two enzymes into the same bilayer. Antibody inhibition experiments coupled with antigen competition indicated a requirement for soluble NSF attachment protein receptor (SNARE) proteins Tlg1p, Tlg2p, and Vti1p in this reaction. Membrane fusion also required the rab protein Vps21p. Vps21p was sufficient if present on either the Kex2p or Ste13p membranes alone, indicative of an inherent symmetry in the reaction. These results identify roles for a Tlg SNARE complex composed of Tlg1p, Tlg2p, Vti1p, and the rab Vps21p in this previously uncharacterized homotypic TGN fusion reaction.</jats:p>",
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