Abstract
Intracellular membrane trafficking depends on the ordered formation and consumption of transport intermediates and requires that membranes fuse with each other in a tightly regulated and highly specific manner. Membrane anchored SNAREs assemble into SNARE complexes that bring membranes together to promote fusion. SNAP29 is a ubiquitous synaptosomal-associated SNARE protein. It interacts with several syntaxins and with the EH domain containing protein EHD1. Loss of functional SNAP29 results in CEDNIK syndrome (Cerebral Dysgenesis, Neuropathy, Ichthyosis and Keratoderma). Using fibroblast cell lines derived from CEDNIK patients, we show that SNAP29 mediates endocytic recycling of transferrin and β1-integrin. Impaired β1-integrin recycling affected cell motility, as reflected by changes in cell spreading and wound healing. No major changes were detected in exocytosis of VSVG protein from the Golgi apparatus, although the Golgi system acquired a dispersed morphology in SNAP29 deficient cells. Our results emphasize the importance of SNAP29 mediated membrane fusion in endocytic recycling and consequently, in cell motility.
Highlights
In eukaryotic cells, intracellular protein trafficking is based on vesicular transport in which cargo molecules are transferred from ‘‘donor’’ compartments to targeted specific ‘‘acceptor’’ compartments
SNAP proteins are t-SNAREs that participate in fusion processes during endocytosis and exocytosis [3,38]
Ample work has been published on the importance of SNAP25, a neuronal SNAP, in regulating neurotransmitter release and modulating calcium dynamics in response to depolarization [39,40]
Summary
Intracellular protein trafficking is based on vesicular transport in which cargo molecules are transferred from ‘‘donor’’ compartments to targeted specific ‘‘acceptor’’ compartments. This complex transport requires vesicle budding and fusion [1]. Transport vesicles carry a specific v-SNARE that binds to cognate tSNAREs to form a trans-SNARE complex (SNAREpin), which becomes a cis-SNARE complex in the fused membrane [3]. The stable cis-SNARE core complex is subsequently dissociated by the action of a-SNAP and the ATPase N-ethylmaleimidesensitive factor (NSF) [4]. SNAREs perform two major functions: they promote vesicle fusion and ensure the specificity of the process
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