Member database | PROSITE profiles |
PROSITE profiles type | domain |
Short name | T_SNARE |
Description
The process of vesicular membrane fusion in eukaryotic cells depends on a
conserved fusion machinery called SNARE (soluble N-ethylmaleimide-sensitive
factor (NSF) attachment protein (SNAP) receptors). In the process of vesicle
docking, proteins present on the vesicle (v-SNARE) have to bind to their
counterpart on the target membrane (t-SNARE) to form a core complex that can
then recruit the soluble proteins NSF and SNAP. This so called fusion complex
can then disassemble after ATP hydrolysis mediated by the ATPase NSF in a
process that leads to membrane fusion and the release of the vesicle contents.
t-SNAREs consist of two different families of proteins: the type II integral
membrane proteins syntaxins and SNAP-25 (synaptosome-associated protein of 25
kDa), which is anchored in the plasma membrane by attached lipids and does not
span the membrane
[1].
The N- and C-terminal coiled-coil domains of members of the SNAP-25 family and
the most C-terminal coiled-coil domain of the syntaxin family are related to
each other and form a new homology domain of approximately 60 amino acids.
This domain is also found in other known proteins involved in vesicular
membrane traffic, some of which belong to different protein families
[1]:
- Yeast SFT1, UFE1, BET1, VAM7 and YDR468c proteins.
- Mammalian TSL-4 proteins.
The profile we developed covers the entire t-SNARE coiled-coil homology
domain.
References
1.A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Weimbs T, Low SH, Chapin SJ, Mostov KE, Bucher P, Hofmann K. Proc. Natl. Acad. Sci. U.S.A. 94, 3046-51, (1997). View articlePMID: 9096343
Integrated to
External Links
Representative structure
1gl2: Crystal structure of an endosomal SNARE core complex