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Exocytosis of Nonclassical Neurotransmitters
Published in Tian-Le Xu, Long-Jun Wu, Nonclassical Ion Channels in the Nervous System, 2021
Xiao Su, Vincent R. Mirabella, Kenneth G. Paradiso, Zhiping P. Pang
Ca2 binding to Syt triggers fusion by binding to SNARE complexes and phospholipids (Figure 6.1). Interestingly, the C2A and C2B domains contribute unequally to regulate vesicle exocytosis. Blocking Ca2+ from binding to the C2B domain blocks over 95% of synchronous exocytosis (Mackler et al., 2002) while blocking Ca2+ from binding to the C2A domain decreases around 40% of exocytosis and also caused a significant decrease in apparent Ca2+ cooperativity of release (Shin et al., 2009). Although the C2A domain is not required for release, Ca2+ binding to the C2A domain significantly contributes to the regulation of overall Ca2+ cooperativity and the triggering of neurotransmitter release. Biochemically, Ca2+ binding to the C2B domain primarily determines binding to phospholipids and displacing of complexin from SNARE trans complexes.
Homeostasis of Dopamine
Published in Nira Ben-Jonathan, Dopamine, 2020
The SNARE complex is formed by members of the synaptosomal-associated protein 25 (SNAP-25), vesicle-associated membrane protein (VAMP) and members of the syntaxins family. Interactions between these proteins create a four-helix bundle, formed by two helices of SNAP-25, one vesicular-transmembrane VAMP and one presynaptic plasma membrane syntaxin that brings together the vesicular and plasmatic membranes. Other proteins that interact with the SNARE complex include Munc-18, complexin, synaptophysin, and synaptotagmin [77]. In addition, synaptotagmin serves as a calcium sensor and regulates the SNARE zipping. The SM proteins are evolutionary conserved cytosolic proteins that serve as essential partners for SNARE proteins in fusion. Among these is Munc 18, which primarily interacts with syntaxin-1 and whose function is tightly regulated by calcium.
Quantitative proteomic analysis to the first commercialized liposomal paclitaxel nano-platform Lipusu revealed the molecular mechanism of the enhanced anti-tumor effect
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2018
Minzhi Zhao, Haiyun Li, Linyang Fan, Yan Ma, He Gong, Wenjia Lai, Qiaojun Fang, Zhiyuan Hu
SLC12A2, also named basolateral Na–K–Cl symporter or bumetanide-sensitive sodium–(potassium)–chloride cotransporter-1 (NKCC1) mediates sodium and chloride reabsorption. It plays a vital role in the regulation of ionic balance and cell volume [22–24]. It had been reported that Na–K–2Cl cotransporter inhibition impaired human lung cellular proliferation by impeded G1-S phase transition [25]. There was a study about NKCC1 as a potential therapeutic target to inhibit hepatocellular carcinoma cell growth and metastasis [26]. CPLX2 positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. It plays a positive role in Ca2+-triggered exocytosis by facilitating vesicle priming [27]. Complexin-2 is regarded as a potential prognostic biomarker in human lung high-grade neuroendocrine tumors [28].
Modulation of neuromuscular synapses and contraction in Drosophila 3rd instar larvae
Published in Journal of Neurogenetics, 2018
Kiel G. Ormerod, JaeHwan Jung, A. Joffre Mercier
Drosophila genes encode eight Dilps, which play roles in life span, reproduction, development, organ growth, diapause and metabolism (Garelli et al., 2015; Nässel & Winther, 2010). Dilps 1–7 act through one receptor, DInr, and Dilp 8 acts through the neuronal relaxin receptor, Lgr3 (Brogiolo et al., 2001; Garelli et al., 2015). In larvae, Dilps 2, 3 and 5 are expressed in cells projecting to neurohemal areas, Dilp 7 is expressed in the abodominal nerve cord, and GFP-labeled Dilp 2 can be released from terminals of motor axons (Brogiolo et al., 2001; Wong et al., 2012). Dilps are present in axon terminals on muscle 12 and DInr is expressed in the muscle fibers (Gorczyca et al., 1993), but no modulatory effects of Dilps on larval synapses have been reported. In adults, diet-induced increases in insulin signaling increase expression of the synaptic protein, Complexin, which, in turn, reduces transmitter release from motor neurons onto CM9 muscles of the proboscis (Mahoney, Azpurua, & Eaton, 2016). Investigating similar effects in larvae might be fruitful.
Common and specific genes and peripheral biomarkers in children and adults with attention-deficit/hyperactivity disorder
Published in The World Journal of Biological Psychiatry, 2018
Cristian Bonvicini, Stephen V. Faraone, Catia Scassellati
Other SNARE genes. Guan et al. (2009) assessed SYP (synaptophysin), STX1A (syntaxin 1A), SYT1 (synaptotagmin 1) and VAMP2 (vesicle-associated membrane protein 2) and found that SYP was associated with cADHD in a Chinese population. Liu et al. (2013a) replicated this result in a larger sample of Han Chinese subjects. Other studies showed prevalently negative findings. The gene CPLX2 (complexin 2) was investigated by Sánchez-Mora et al. (2013a), who reported a significant association (Table S1).