Authors: | McNew, J. A.; Weber, T.; Engelman, D. M.; Söllner, T. H.; Rothman, J. E. |
Article Title: | The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion |
Abstract: | The topology of a SNARE complex bridging two docked vesicles could act as a mechanical couple to do work on the lipid bilayer resulting in fusion. To test this, we prepared a series of modified SNARE proteins and determined their effects on SNARE-dependent membrane fusion. When two helix-breaking proline residues are introduced into the juxtamembrane region of VAMP, there is little or no effect on fusion, and the same change in syntaxin 1A only reduced the extent and rate of fusion by half. The insertion of a flexible linker between the transmembrane domain and the conserved coiled-coil domain only moderately affected fusion; however, fusion efficiency systematically decreased with increasing length of the linker. Together, these results rule out a requirement for helical continuity and suggest that distance is a critical factor for membrane fusion. |
Keywords: | nerve tissue proteins; membrane proteins; structure activity relation; amino acid sequence; molecular sequence data; carrier proteins; recombinant proteins; pliability; mutagenesis, site-directed; structure analysis; protein structure, secondary; antigens, surface; proline; vesicular transport proteins; receptor protein; membrane fusion; membrane structure; syntaxin; protein quaternary structure; syntaxin 1; r-snare proteins; snare proteins; proline derivative; synaptosomal-associated protein 25; article |
Journal Title: | Molecular Cell |
Volume: | 4 |
Issue: | 3 |
ISSN: | 1097-2765 |
Publisher: | Cell Press |
Date Published: | 1999-09-01 |
Start Page: | 415 |
End Page: | 421 |
Language: | English |
DOI: | 10.1016/s1097-2765(00)80343-3 |
PUBMED: | 10518222 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |