ArticleBiochemistry and biophysics reports2024
SIP30 involvement in vesicle exocytosis from PC12 cells.
Article in Biochemistry and biophysics reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 2 citations in OpenAlex.
- Integrating AlphaFold2, RoseTTAFold2, and HADDOCK to refine Protein-Protein Interaction (PPI) candidate selection: A case study with ZWINT.Biochemistry and biophysics reports · 2026Article
- Outer kinetochore proteins form linear elements to regulate vesicle transport.Journal of cell science · 2026Article
- Phylogenetic analysis of mammalian SIP30 sequences indicating accelerated adaptation of functional domain in primates.Biochemistry and biophysics reports · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
SNAP25 (synaptosome-associated protein of 25 kDa) is a core SNARE (soluble N-ethylmaleimide-sensitive factor attachment receptor) protein; and the interaction between SNAP25 and other SNARE proteins is essential for synaptic vesicle exocytosis. Identified as a SNAP25 interacting protein, SIP30 (SNAP25 interacting protein at 30 kDa) has been shown to modulate neuropathic pain behavior, and is potentially involved in the cellular process of vesicle exocytosis. Previous study demonstrated that using a vesicle secretion assay in PC12 cells, anti-SIP30 siRNA reduced vesicle exocytosis. We investigated vesicle exocytosis from PC12 cells with FM1-43 fluorescence dye, and demonstrated that anti-SIP30 siRNA reduced the pool of releasable vesicles and the rate of vesicle exocytosis, without affecting the endocytosis and recycling of the exocytosed vesicles. The results show that SIP30 is involved in vesicle exocytosis, suggesting a potential mechanism of SIP30 modulation of neuropathic pain.
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