QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Search for Related Content

A catalyst for SNARE assembly

Members of the Munc 18/Sec1 family, such as Sly 1p, play essential roles in membrane trafficking. The proteins bind to t-SNAREs (components of the SNARE complexes that drive membrane fusion); however, their exact role is far from clear, since some experiments suggest that they can inhibit membrane fusion. Koji Yoda and co-workers now demonstrate that Sly 1p directly stimulates SNARE assembly (see p. 3683). They show that the interaction between Sly 1p and the t-SNARE Sed5p is significantly reduced in a temperature-sensitive Sly1^ts mutant and that Sly1p^ts protein has a lower affinity for Sed5p than does its wild-type counterpart. Most significant, however, is the authors' use of a novel in vitro assay for SNARE complex assembly in Sly1^ts mutant lysates, in which they show that purified Sly1 protein stimulates the formation of trans-SNARE complexes involving Sed5p and its partner the v-SNARE Bet1p. Since Sly1p-Sed5p binding is unaffected by SNARE complex formation, Yoda and co-workers propose that Sly1p acts prior to complex formation; the Munc 18/Sec1 family might thus function by binding to t-SNAREs and inducing a `pro-v-SNARE' binding state.

Related articles in JCS:

Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex

Yoichi Kosodo, Yoichi Noda, Hiroyuki Adachi, and Koji Yoda
JCS 2002 115: 3683-3691. [Abstract] [Full Text]  

This article has been cited by other articles:

				M Hinkins, J Huntriss, D Miller, and H M Picton Expression of Polycomb-group genes in human ovarian follicles, oocytes and preimplantation embryos Reproduction, December 1, 2005; 130(6): 883 - 888. [Abstract] [Full Text] [PDF]

				D. Peters, J. Freund, and R. L. Ochs Genome-wide transcriptional analysis of carboplatin response in chemosensitive and chemoresistant ovarian cancer cells Mol. Cancer Ther., October 1, 2005; 4(10): 1605 - 1616. [Abstract] [Full Text] [PDF]

				S. A. Grigoryev, T. Nikitina, J. R. Pehrson, P. B. Singh, and C. L. Woodcock Dynamic relocation of epigenetic chromatin markers reveals an active role of constitutive heterochromatin in the transition from proliferation to quiescence J. Cell Sci., December 1, 2004; 117(25): 6153 - 6162. [Abstract] [Full Text] [PDF]

				N. E. Istomina, S. S. Shushanov, E. M. Springhetti, V. L. Karpov, I. A. Krasheninnikov, K. Stevens, K. S. Zaret, P. B. Singh, and S. A. Grigoryev Insulation of the Chicken {beta}-Globin Chromosomal Domain from a Chromatin-Condensing Protein, MENT Mol. Cell. Biol., September 15, 2003; 23(18): 6455 - 6468. [Abstract] [Full Text] [PDF]

				S. A. Grigoryev, T. Nikitina, J. R. Pehrson, P. B. Singh, and C. L. Woodcock Dynamic relocation of epigenetic chromatin markers reveals an active role of constitutive heterochromatin in the transition from proliferation to quiescence J. Cell Sci., December 1, 2004; 117(25): 6153 - 6162. [Abstract] [Full Text] [PDF]

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Search for Related Content