JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 550K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Elkind, N. B.
Right arrow Articles by Novick, P. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Elkind, N. B.
Right arrow Articles by Novick, P. J.
Right arrowPubmed/NCBI databases
*Gene*Genome
*GEO Profiles*HomoloGene
*Protein
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2000//95 $5.00
The Journal of Cell Biology, Volume 149, Number 1, , 2000 95-110

Original Article

The Role of the Cooh Terminus of Sec2p in the Transport of Post-Golgi Vesicles



N. Barry Elkinda, Christiane Walch-Solimenaa, and Peter J. Novicka

a Department of Cell Biology, Yale University, New Haven, Connecticut, 06510
Yale University School of Medicine, Department of Cell Biology, Sterling Hall of Medicine, 333 Cedar St., New Haven, CT 06520-8002.(203) 785-7226(203) 785-5871

peter.novick{at}yale.edu

Sec2p is required for the polarized transport of secretory vesicles in S. cerevisiae. The Sec2p NH2 terminus encodes an exchange factor for the Rab protein Sec4p. Sec2p associates with vesicles and in Sec2p COOH-terminal mutants Sec4p and vesicles no longer accumulate at bud tips. Thus, the Sec2p COOH terminus functions in targeting vesicles, however, the mechanism of function is unknown. We found comparable exchange activity for truncated and full-length Sec2 proteins, implying that the COOH terminus does not alter the exchange rate. Full-length Sec2-GFP, similar to Sec4p, concentrates at bud tips. A COOH-terminal 58–amino acid domain is necessary but not sufficient for localization. Sec2p localization depends on actin, Myo2p and Sec1p, Sec6p, and Sec9p function. Full-length, but not COOH-terminally truncated Sec2 proteins are enriched on membranes. Membrane association of full-length Sec2p is reduced in sec6-4 and sec9-4 backgrounds at 37°C but unaffected at 25°C. Taken together, these data correlate loss of localization of Sec2 proteins with reduced membrane association. In addition, Sec2p membrane attachment is substantially Sec4p independent, supporting the notion that Sec2p interacts with membranes via an unidentified Sec2p receptor, which would increase the accessibility of Sec2p exchange activity for Sec4p.

Key Words: transport • exchange factor • yeast • Rab • vesicles

© 2000 The Rockefeller University Press

Abbreviations used in this paper: GFP, green fluorescent protein; LAT, latrunculin; sec, secretory.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents