Abstract
Despite extensive study, regulation of membrane trafficking is incompletely understood. In particular, the specific role of SNARE (Soluble NSF Attachment REceptor) proteins for distinct trafficking steps and their mechanism of action, beyond the core function in membrane fusion, are still elusive. Snap29 is a SNARE protein related to Snap25 that gathered a lot of attention in recent years. Here, we review the study of Snap29 and its emerging involvement in autophagy, a self eating process that is key to cell adaptation to changing environments, and in other trafficking pathways. We also discuss Snap29 role in synaptic transmission and in cell division, which might extend the repertoire of SNARE-mediated functions. Finally, we present evidence connecting Snap29 to human disease, highlighting the importance of Snap29 function in tissue development and homeostasis.
Highlights
The specialized trafficking routes that evolved between compartments of the endomembrane system rely on a wide set of proteins, including primarily soluble N-ethylmaleimidesensitive-factor attachment receptor (SNARE), Rab GTPases and a large set of effectors and tethering factors, that ensure specificity of cargo delivery to a wide range of different target compartments
In pupal salivary glands, which secrete large amounts of granule containing glue, excess granules are cleared by lysosomes in a specialized form of autophagy termed crynophagy which was found to be lost upon depletion of Syx13, Snap29, Vamp7, the GTPase Rab2 and Rab7 and components of the homotypic fusion and protein sorting (HOPS) tethering complex (Fig. 4C)
In the 20 years after Snap29 discovery, multiple studies have revealed a wide range of cellular processes controlled by the SNARE
Summary
The specialized trafficking routes that evolved between compartments of the endomembrane system rely on a wide set of proteins, including primarily SNAREs, Rab GTPases and a large set of effectors and tethering factors, that ensure specificity of cargo delivery to a wide range of different target compartments. All proteins of the 4-helix bundle are associated to the target membrane, in an arrangement often called cis-SNARE complex, that is disassembled by the activity of a number of proteins including
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