Functional architecture of an intracellular membrane t-SNARE

Ryouichi Fukuda, James A. McNew, Thomas Weber, Francesco Parlati, Thomas Engel, Walter Nickel, James E. Rothman and Thomas H. Söllner ()
Additional contact information
Ryouichi Fukuda: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
James A. McNew: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
Thomas Weber: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
Francesco Parlati: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
Thomas Engel: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
Walter Nickel: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
James E. Rothman: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center
Thomas H. Söllner: Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center

Nature, 2000, vol. 407, issue 6801, 198-202

Abstract: Abstract Lipid bilayer fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs)1,2. The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, of which one is supplied by the v-SNARE and the other three by the t-SNARE3. For t-SNAREs on the plasma membrane, the protein syntaxin4 supplies one helix and a SNAP-25 protein5 contributes the other two. Although there are numerous homologues of syntaxin on intracellular membranes6, there are only two SNAP-25-related proteins in yeast, Sec9 and Spo20, both of which are localized to the plasma membrane and function in secretion7 and sporulation8, respectively. What replaces SNAP-25 in t-SNAREs of intracellular membranes? Here we show that an intracellular t-SNARE is built from a ‘heavy chain’ homologous to syntaxin and two separate non-syntaxin ‘light chains’. SNAP-25 may thus be the exception rather than the rule, having been derived from genes that encoded separate light chains that fused during evolution to produce a single gene encoding one protein with two helices.

Date: 2000
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/35025084 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:407:y:2000:i:6801:d:10.1038_35025084

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35025084

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().