ArticleBioscience reports2009
Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs.
Article in Bioscience reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Lytic granule exocytosis at immune synapses: lessons from neuronal synapses.Frontiers in immunology · 2023Review
- Interaction between the VP2 protein of deformed wing virus and host snapin protein and its effect on viral replication.Frontiers in microbiology · 2023Article
- Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019Review
- Neurodevelopmental disease mechanisms, primary cilia, and endosomes converge on the BLOC-1 and BORC complexes.Developmental neurobiology · 2018Review
- SNAPIN is critical for lysosomal acidification and autophagosome maturation in macrophages.Autophagy · 2017Article
- STX13 regulates cargo delivery from recycling endosomes during melanosome biogenesis.Journal of cell science · 2015Article
- LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25.Experimental & molecular medicine · 2013Article
- Beclin-1-interacting autophagy protein Atg14L targets the SNARE-associated protein Snapin to coordinate endocytic trafficking.Journal of cell science · 2012Article
- Snapin is critical for presynaptic homeostatic plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Article
- Cell biology of the BLOC-1 complex subunit dysbindin, a schizophrenia susceptibility gene.Molecular neurobiology · 2011Review
- Snapin deficiency is associated with developmental defects of the central nervous system.Bioscience reports · 2011Article
- Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons.Neuron · 2010Article
- Targeting of the GTPase Irgm1 to the phagosomal membrane via PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3) promotes immunity to mycobacteria.Nature immunology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Late endocytic membrane trafficking delivers target materials and newly synthesized hydrolases into lysosomes and is critical for maintaining an efficient degradation process and cellular homoeostasis. Although some features of late endosome-lysosome trafficking have been described, the mechanisms underlying regulation of this event remain to be elucidated. Our previous studies showed that Snapin, as a SNAP25 (25 kDa synaptosome-associated protein)-binding protein, plays a critical role in priming synaptic vesicles for synchronized fusion in neurons. In the present study, we report that Snapin also associates with late endocytic membranous organelles and interacts with the late endosome-targeted SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) complex. Using a genetic mouse model, we further discovered that Snapin is required to maintain a proper balance of the late endocytic protein LAMP-1 (lysosome-associated membrane protein-1) and late endosomal SNARE proteins syntaxin 8 and Vti1b (vesicle transport through interaction with target SNAREs homologue 1b). Deleting the snapin gene in mice selectively led to the accumulation of these proteins in late endocytic organelles. Thus our present study suggests that Snapin serves as an important regulator of the late endocytic fusion machinery, in addition to its established role in regulating synaptic vesicle fusion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.