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Vesicle transport through interaction with t-SNAREs 1a (Vti1a)'s roles in neurons.

ABSTRACT: The Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family mediates membrane fusion during membrane trafficking and autophagy in all eukaryotic cells, with a number of SNAREs having cell type-specific functions. The endosome-trans-Golgi network (TGN) localized SNARE, Vesicle transport through interaction with t-SNAREs 1A (Vti1a), is unique among SNAREs in that it has numerous neuron-specific functions. These include neurite outgrowth, nervous system development, spontaneous neurotransmission, synaptic vesicle and dense core vesicle secretion, as well as a process of unconventional surface transport of the Kv4 potassium channel. Furthermore, the human VT11A gene is known to form fusion products with neighboring genes in cancer tissues, and VT11A variants are associated with risk in cancers, including glioma. In this review, I highlight VTI1A's known physio-pathological roles in brain neurons, as well as unanswered questions in these regards.

SUBMITTER: Tang BL

PROVIDER: S-EPMC7398939 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Vesicle transport through interaction with t-SNAREs 1a (Vti1a)'s roles in neurons.

Tang Bor Luen BL

Heliyon 20200801 8

The Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family mediates membrane fusion during membrane trafficking and autophagy in all eukaryotic cells, with a number of SNAREs having cell type-specific functions. The endosome-<i>trans</i>-Golgi network (TGN) localized SNARE, Vesicle transport through interaction with t-SNAREs 1A (Vti1a), is unique among SNAREs in that it has numerous neuron-specific functions. These include neurite outgrowth, nervous system developme ...[more]

PMID: 32775753

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Project description:Background Neurons are highly specialized cells with a complex morphology generated by various membrane trafficking steps. They contain Golgi outposts in dendrites, which are formed from somatic Golgi tubules. In trafficking membrane fusion is mediated by a specific combination of SNARE proteins. A functional SNARE complex contains four different helices, one from each SNARE subfamily (R-, Qa, Qb and Qc). Loss of the two Qb SNAREs vti1a and vti1b from the Golgi apparatus and endosomes leads to death at birth in mice with massive neurodegeneration in peripheral ganglia and defective axon tracts. Methods Hippocampal and cortical neurons were isolated from Vti1a−/−Vti1b−/− double deficient, Vti1a−/−Vti1b+/−, Vti1a+/−Vti1b−/− and Vti1a+/−Vti1b+/− double heterozygous embryos. Neurite outgrowth was determined in cortical neurons and after stimulation with several neurotrophic factors or the Rho-associated protein kinase ROCK inhibitor Y27632, which induces exocytosis of enlargeosomes, in hippocampal neurons. Moreover, postsynaptic densities were isolated from embryonic Vti1a−/−Vti1b−/− and Vti1a+/−Vti1b+/− control forebrains and analyzed by western blotting. Results Golgi outposts were present in Vti1a−/−Vti1b+/− and Vti1a+/−Vti1b−/− dendrites of hippocampal neurons but not detected in the absence of vti1a and vti1b. The length of neurites was significantly shorter in double deficient cortical neurons. These defects were not observed in Vti1a−/−Vti1b+/− and Vti1a+/−Vti1b−/− neurons. NGF, BDNF, NT-3, GDNF or Y27632 as stimulator of enlargeosome secretion did not increase the neurite length in double deficient hippocampal neurons. Vti1a−/−Vti1b−/− postsynaptic densities contained similar amounts of scaffold proteins, AMPA receptors and NMDA receptors compared to Vti1a+/−Vti1b+/−, but much more TrkB, which is the receptor for BDNF. Conclusion The absence of Golgi outposts did not affect the amount of AMPA and NMDA receptors in postsynaptic densities. Even though TrkB was enriched, BDNF was not able to stimulate neurite elongation in Vti1a−/−Vti1b−/− neurons. Vti1a or vti1b function as the missing Qb-SNARE together with VAMP-4 (R-SNARE), syntaxin 16 (Qa-SNARE) and syntaxin 6 (Qc-SNARE) in induced neurite outgrowth. Our data show the importance of vti1a or vti1b for two pathways of neurite elongation. Supplementary Information The online version contains supplementary material available at 10.1186/s13064-022-00168-2.

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Vesicle transport through interaction with t-SNAREs 1a (Vti1a)'s roles in neurons.

Publications

Vesicle transport through interaction with t-SNAREs 1a (Vti1a)'s roles in neurons.

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