VAMP subfamilies identified by specific R-SNARE motifs.
VAMP subfamilies identified by specific R-SNARE motifs.
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DOI：
10.1016/j.biolcel.2003.12.009
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发表时间：
2004-05
影响因子：
2.7
通讯作者：
V. Rossi;Raffaella Picco;M. Vacca;M. D'Esposito;M. D'urso;T. Galli;F. Filippini
中科院分区：
文献类型：
--
作者：
V. Rossi;Raffaella Picco;M. Vacca;M. D'Esposito;M. D'urso;T. Galli;F. Filippini
Summry—In eukaryotes, interactions among the α‐helical coiled‐coil domains (CCDs) of soluble N‐ethylmaleimide‐sensitive factor attachment protein receptors (SNAREs) play a pivotal role in mediating the fusion among vesicles and target membranes. Surface residues of such CCDs are major candidates to regulate the specificity of membrane fusion, as they may alter local charge at the interaction layers and surface of the fusion complex, possibly modulating its formation and/or the binding of non‐SNARE regulatory factors. Based on alternate patterns in surface residues, we have identified two motifs which group vesicular SNAREs in two novel subfamilies: RG‐SNAREs and RD‐SNAREs. The RG‐SNARE CCD is common to all members of the widely conserved family of long VAMPs or longins and to yeast and non‐neuronal VAMPs, possibly mediating “basic” fusion mechanisms; instead, only synaptobrevins from Bilateria share an RD‐SNARE CCD, which is likely to mediate interactions to specific, yet unknown, regulatory factors and/or be the landmark of rapid fusion reactions like that mediating the release of neurotransmitters.
