ArticlePloS one2014
Tomosyn interacts with the SUMO E3 ligase PIASγ.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The Role of Tomosyn in the Regulation of Neurotransmitter Release.Advances in neurobiology · 2023Article
- SUMO: From Bench to Bedside.Physiological reviews · 2020Review
- The ubiquitin-proteasome system functionally links neuronal Tomosyn-1 to dendritic morphology.The Journal of biological chemistry · 2018Article
- SUMOylation and calcium control syntaxin-1A and secretagogin sequestration by tomosyn to regulate insulin exocytosis in human ß cells.Scientific reports · 2017Article
- Isocitrate-to-SENP1 signaling amplifies insulin secretion and rescues dysfunctional β cells.The Journal of clinical investigation · 2015Article
- How do reducing equivalents increase insulin secretion?The Journal of clinical investigation · 2015Article
- SUMOylation of synapsin Ia maintains synaptic vesicle availability and is reduced in an autism mutation.Nature communications · 2015Article
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Authors and funding
5 authors.
Funding
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Abstract
Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment Protein Receptor) proteins to regulate neurotransmission and is one of the few neuronal SUMO substrate proteins identified. Here we used yeast two-hybrid screening to show that tomosyn-1 interacts with the SUMO E3 ligase PIASγ (Protein Inhibitor of Activated STAT; PIAS4 or ZMIZ6). This novel interaction involved the C-terminus of tomosyn-1 and the N-terminus of PIASγ. It was confirmed by two-way immunoprecipitation experiments using the full-length proteins expressed in HEK293T cells. Tomosyn-1 was preferentially modified by the SUMO-2/3 isoform. PIASγ-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.
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Registered trials
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