References
- Baldelli, P., Fassio, A., Valtorta, F., and Benfenati, F. (2007). Lack of synapsin I reduces the readily releasable pool of synaptic vesicles at central inhibitory synapses. J. Neurosci. 27, 13520-13531. https://doi.org/10.1523/JNEUROSCI.3151-07.2007
- Brautigam, C.A., Chelliah, Y., and Deisenhofer, J. (2004). Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I. J. Biol. Chem., 279, 11948-11956. https://doi.org/10.1074/jbc.M312015200
- Cavalleri, G.L., Weale, M.E., Shianna, K.V., Singh, R., Lynch, J.M., Grinton, B., Szoeke, C., Murphy, K., Kinirons, P., O'Rourke, D., et al. (2007). Multicentre search for genetic susceptibility loci in sporadic epilepsy syndrome and seizure types: a case-control study. Lancet Neurol. 6, 970-980. https://doi.org/10.1016/S1474-4422(07)70247-8
- Cheetham, J.J., Hilfiker, S., Benfenati, F., Weber, T., Greengard, P., and Czernik, A.J. (2001). Identification of synapsin I peptides that insert into lipid membranes. Biochem. J. 354, 57-66. https://doi.org/10.1042/bj3540057
- Chi, P., Greengard, P., and Ryan, T.A. (2003). Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies. Neuron 38, 69-78. https://doi.org/10.1016/S0896-6273(03)00151-X
- Dyck, B.A., Beyaert, M.G., Ferro, M.A., and Mishra, R.K. (2011). Medial prefrontal cortical synapsin II knock-down induces behavioral abnormalities in the rat: examining synapsin II in the pathophysiology of schizophrenia. Schizophr Res. 130, 250-259. https://doi.org/10.1016/j.schres.2011.05.017
- Esser, L., Wang, C.R., Hosaka, M., Smagula, C.S., C.Südhof, T.C., and Deisenhofer, J. (1998). Synapsin I is structurally similar to ATP-utilizing enzymes. EMBO J. 17, 977-984. https://doi.org/10.1093/emboj/17.4.977
- Evergren, E., Marcucci, M., Tomilin, N., Low, P., Slepnev, V., Andersson, F., Gad, H., Brodin, L., De Camilli, P., and Shupliakov, O. (2004). Amphiphysin is a component of clathrin coats formed during synaptic vesicle recycling at the lamprey giant synapse. Traffic 5, 514-528. https://doi.org/10.1111/j.1398-9219.2004.00198.x
- Feng, J., Chi, P., Blanpied, T.A, Xu, Y., Magarinos, A.M., Ferreira, A., Takahashi, R.H., Kao, H.-T., McEwen, B.S., Ryan, T.A., et al. (2002). Regulation of neurotransmitter release by synapsin III. J. Neurosci. 22, 4372-4380. https://doi.org/10.1523/JNEUROSCI.22-11-04372.2002
- Garcia, C.C., Blair, H.J., Seager, M., Coulthard, A., Tennant, S., Buddles, M., Curtis, A., and Goodship, J.A. (2004). Identification of a mutation in synapsin I, a synaptic vesicle protein, in a family with epilepsy. J. Med. Genet. 41,183-186. https://doi.org/10.1136/jmg.2003.013680
- Giovedì, S., Darchen, F., Valtorta, F., Greengard, P., and Benfenati, F. (2004). Synapsin is a novel Rab3 effector protein on small synaptic vesicles: II. Functional effects of the Rab3A-synapsin I interaction. J. Biol. Chem. 279, 43769-43779. https://doi.org/10.1074/jbc.M404168200
- Gitler, D., Xu, Y., Kao, H.-T., Lin, D., Lim, S., Feng, J., Greengard, P., and Augustine, G.J. (2004a). Molecular determinants of synapsin targeting to presynaptic terminals. J. Neurosci. 24, 3711-3720. https://doi.org/10.1523/JNEUROSCI.5225-03.2004
- Gitler, D., Takagishi, Y., Feng, J., Ren, Y., Rodriguiz, R.M., Wetsel, W.C., Greengard, P., and Augustine, G.J. (2004b). Different presynaptic roles of synapsins at excitatory and inhibitory synapses. J. Neurosci. 24, 11368-11380. https://doi.org/10.1523/JNEUROSCI.3795-04.2004
- Gitler, D., Cheng, Q., Greengard, P., and Augustine, G.J. (2008). Synapsin IIa controls the reserve pool of glutamatergic synaptic vesicles. J. Neurosci. 28, 10835-10843. https://doi.org/10.1523/JNEUROSCI.0924-08.2008
- Hilfiker, S., Schweizer, F.E., Kao, H.T., Czernik, A.J., Greengard, P., and Augustine, G.J. (1998). Two sites of action for synapsin domain E in regulating neurotransmitter release. Nat. Neurosci. 1, 29-35. https://doi.org/10.1038/229
- Hilfiker, S., Pieribone, V.A., Czernik, A.J., Kao, H.T., Augustine, G.J., and Greengard, P. (1999). Synapsins as regulators of neurotransmitter release. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 354, 269-279. https://doi.org/10.1098/rstb.1999.0378
- Hilfiker, S., Benfenati, F., Doussau, F., Nairn, A.C., Czernik, A.J., Augustine, G.J., and Greengard, P. (2005). Structural domains involved in the regulation of transmitter release by synapsins. J. Neurosci. 25, 2658-2669. https://doi.org/10.1523/JNEUROSCI.4278-04.2005
-
Hosaka, M., and Südhof, T.C. (1998). Synapsin III, a Novel Synapsin with an Unusual Regulation by
$Ca^{2+}$ . J. Biol. Chem. 273, 13371-13374. https://doi.org/10.1074/jbc.273.22.13371 - Hosaka, M., and Südhof, T.C. (1999). Homo- and heterodimerization of synapsins. J. Biol. Chem. 274, 16747-16753. https://doi.org/10.1074/jbc.274.24.16747
- Jovanovic, J.N., Benfenati, F., Siow, Y.L., Sihra, T.S., Sanghera, J.S., Pelech, S.L., Greengard, P., and Czernik, A.J. (1996). Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions. Proc. Natl. Acad. Sci. USA 93, 3679-3683. https://doi.org/10.1073/pnas.93.8.3679
- Kao, H.T., Porton, B., Czernik, A. J., Feng, J., Yiu, G., Haring, M., Benfenati, F., and Greengard, P. (1998). A third member of the synapsin gene family. Proc. Natl. Acad. Sci. USA 95, 4667-4672. https://doi.org/10.1073/pnas.95.8.4667
- Kile, B.M., Guillot, T.S., Venton, B.J., Wetsel, W.C., Augustine, G.J., and Wightman, R.M. (2010). Synapsins differentially control dopamine and serotonin release. J. Neurosci. 30, 9762-9770. https://doi.org/10.1523/JNEUROSCI.2071-09.2010
- Li, L., Chin, L.S., Shupliakov, O., Brodin, L., Sihra, T.S., Hvalby, O., Jensen, V., Zheng, D.,McNamara, J.O., Greengard, P., et al., (1995). Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. Proc. Natl. Acad. Sci. USA 92, 9235-9239. https://doi.org/10.1073/pnas.92.20.9235
-
Llinas, R., Gruner, J.A., Sugimori, M., McGuinness, T.L., Greengard, P. (1991). Regulation by synapsin I and
$Ca^{2+}$ -calmodulindependent protein kinase II of the transmitter release in squid giant synapse. J. Physiol. 436, 257-282. https://doi.org/10.1113/jphysiol.1991.sp018549 - Medrihan, L., Cesca, F., Raimondi, A., Lignani, G., Baldelli, P., and Benfenati, F. (2013). Synapsin II desynchronizes neurotransmitter release at inhibitory synapses by interacting with presynaptic calcium channels. Nat. Commun. 4, 1512. https://doi.org/10.1038/ncomms2515
- Mirnics, K., Middleton, F.A., Marquez, A., Lewis, D.A., Levitt, P. (2000). Molecular characterization of schizophrenia viewed by microarray analysis of gene expression in prefrontal cortex. Neuron 28, 53-67. https://doi.org/10.1016/S0896-6273(00)00085-4
- Monaldi, I., Vassalli, M., Bachi, A., Giovedì, S., Millo, E., Valtorta, F., Raiteri, R., Benfenati, F., and Fassio, A. (2010). The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering. Biochem. J. 426, 55-64. https://doi.org/10.1042/BJ20090762
- Pieribone, V.A., Shupliakov, O., Brodin, L., Hilfiker, S., Czernik, A.J., Greengard, P. (1995) Distinct pools of synaptic vesicles in neurotransmitter release. Nature 375, 493-497. https://doi.org/10.1038/375493a0
- Porton, B., Ferreira, A., DeLisi, L.E., and Kao, H.T. (2004). A rare polymorphism affects a mitogen-activated protein kinase site in synapsin III: Possible relationship to schizophrenia. Biol. Psychiatry 55, 118-125. https://doi.org/10.1016/j.biopsych.2003.07.002
- Porton, B., Wetsel, W.C., Kao, H.T. (2011). Synapsin III: role in neuronal plasticity and disease. Semin Cell Dev. Biol. 22, 416-424. https://doi.org/10.1016/j.semcdb.2011.07.007
- Rosahl, T.W., Spillane, D., Missler, M., Herz, J., Selig, D.K., Wolff, J.R., Hammer, R.E., Malenka, R.C., Sudhof, T.C. (1995). Essential functions of synapsins I and II in synaptic vesicle regulation. Nature 375, 488-493. https://doi.org/10.1038/375488a0
- Song, SH., and Augustine, J.G. (2014). Synapsin isoforms regulating GABA release from hippocampal interneurons. Annual Meeting of Society for Neuroscience 783,12.
- Südhof, T.C., Czernik, A.J., Kao, H.T., Takei, K., Johnston, P.A., Horiuchi, A., Kanazir, S.D., Wagner, M.A., Perin, M.S., and De Camilli, P. (1989). Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins. Science 245, 1474-1480. https://doi.org/10.1126/science.2506642
- Tan, M.L., Dyck, B.A., Gabriele, J., Daya, R.P., Thomas, N., Sookram, C., Basu, D., Ferro, M.A., Chong, V.Z., and Mishra, R.K. (2014). Synapsin II gene expression in the dorsolateral prefrontal cortex of brain specimens from patients with schizophrenia and bipolar disorder: effect of lifetime intake of antipsychotic drugs. Pharmacogenomics J.14, 63-69. https://doi.org/10.1038/tpj.2013.6
- Vawter, M.P., Thatcher, L., Usen, N., Hyde, T.M., Kleinman, J.E., and Freed, W.J. (2002). Reduction of synapsin in the hippocampus of patients with bipolar disorder and schizophrenia. Mol. Psychiatry 7, 571-578. https://doi.org/10.1038/sj.mp.4001158
- Venton, B.J., Seipel, A.T., Phillips, P.E.M., Wetsel, W.C., Gitler, D., Greengard, P., Augustine, G.J., and Wightman, R.M. (2006). Cocaine increases dopamine release by mobilization of a synapsin-dependent reserve pool. J. Neurosci. 26, 3206-3209. https://doi.org/10.1523/JNEUROSCI.4901-04.2006
- Villanueva, M., Thornley, K., Augustine, G.J., and Wightman, R.M. (2006). Synapsin II negatively regulates catecholamine release. Brain Cell Biol. 35, 125-136.
Cited by
- Optimizing neuronal differentiation of human pluripotent NT2 stem cells in monolayer cultures vol.58, pp.8, 2016, https://doi.org/10.1111/dgd.12323
- The mouse pulvinar nucleus: Organization of the tectorecipient zones vol.34, 2017, https://doi.org/10.1017/S0952523817000050
- Analysis of SUMO1-conjugation at synapses vol.6, 2017, https://doi.org/10.7554/eLife.26338
- Poly(N-(4-aminobutyl)-acrylamide) as mimetic polylysine for improving survival and differentiation of cerebellar granule neurons 2017, https://doi.org/10.1002/jbm.b.33932
- PI3K/Akt Pathway is Required for Spinal Central Sensitization in Neuropathic Pain 2018, https://doi.org/10.1007/s10571-017-0541-x
- The Role of Synapsins in Neurological Disorders vol.34, pp.2, 2018, https://doi.org/10.1007/s12264-017-0201-7
- Ryanodine Receptor-Mediated Calcium Release Has a Key Role in Hippocampal LTD Induction vol.12, pp.1662-5102, 2018, https://doi.org/10.3389/fncel.2018.00403
- Molecular Mechanisms of Short-Term Plasticity: Role of Synapsin Phosphorylation in Augmentation and Potentiation of Spontaneous Glutamate Release vol.10, pp.1663-3563, 2018, https://doi.org/10.3389/fnsyn.2018.00033
- Memory enhancing effects of BPN14770, an allosteric inhibitor of phosphodiesterase-4D, in wild-type and humanized mice vol.43, pp.11, 2018, https://doi.org/10.1038/s41386-018-0178-6
- Calcineurin and Its Role in Synaptic Transmission vol.83, pp.6, 2018, https://doi.org/10.1134/S0006297918060056
- Subcutaneous Sustained-Release of Poly-Arginine Ameliorates Cognitive Impairment in a Transgenic Mouse Model of Alzheimer’s Disease vol.07, pp.04, 2018, https://doi.org/10.4236/aad.2018.74011
- Decreased dopamine in striatum and difficult locomotor recovery from MPTP insult after exposure to radiofrequency electromagnetic fields vol.9, pp.1, 2019, https://doi.org/10.1038/s41598-018-37874-z
- Keratan sulfate, a complex glycosaminoglycan with unique functional capability vol.28, pp.4, 2015, https://doi.org/10.1093/glycob/cwy003
- Exercise improves recognition memory and synaptic plasticity in the prefrontal cortex for rats modelling vascular dementia vol.40, pp.1, 2018, https://doi.org/10.1080/01616412.2017.1398389
- Differential Expression of Synapsin I and II upon Treatment by Lithium and Valproic Acid in Various Brain Regions vol.21, pp.6, 2015, https://doi.org/10.1093/ijnp/pyy023
- Protective effects of primary neural stem cell treatment in ischemic stroke models vol.16, pp.3, 2018, https://doi.org/10.3892/etm.2018.6466
- Short-term plasticity at cerebellar granule cell to molecular layer interneuron synapses expands information processing vol.8, pp.None, 2015, https://doi.org/10.7554/elife.41586
- The readily-releasable pool dynamically regulates multivesicular release vol.8, pp.None, 2015, https://doi.org/10.7554/elife.47434
- A proline-rich motif on VGLUT1 reduces synaptic vesicle super-pool and spontaneous release frequency vol.8, pp.None, 2015, https://doi.org/10.7554/elife.50401
- Regulation of Neurotransmitter Release by Amyloid Precursor Protein Through Synapsin Phosphorylation vol.44, pp.3, 2015, https://doi.org/10.1007/s11064-017-2418-2
- Synapsins regulate α-synuclein functions vol.116, pp.23, 2019, https://doi.org/10.1073/pnas.1903054116
- Postsynaptic Mechanisms Render Syn I/II/III Mice Highly Responsive to Psychostimulants vol.22, pp.7, 2015, https://doi.org/10.1093/ijnp/pyz019
- Regular Exercise Enhances Cognitive Function and Intracephalic GLUT Expression in Alzheimer’s Disease Model Mice vol.72, pp.1, 2019, https://doi.org/10.3233/jad-190328
- Synapsins are expressed at neuronal and non-neuronal locations in Octopus vulgaris vol.9, pp.1, 2015, https://doi.org/10.1038/s41598-019-51899-y
- SNARE Complex-Associated Proteins and Alcohol vol.44, pp.1, 2015, https://doi.org/10.1111/acer.14238
- The good and bad of therapeutic strategies that directly target α‐synuclein vol.72, pp.4, 2015, https://doi.org/10.1002/iub.2194
- Going Deep into Synaptic Vesicle Machinery Genes and Migraine Susceptibility – A Case‐Control Association Study vol.60, pp.10, 2020, https://doi.org/10.1111/head.13957
- Synaptic Loss in Multiple Sclerosis: A Systematic Review of Human Post-mortem Studies vol.12, pp.None, 2015, https://doi.org/10.3389/fneur.2021.782599
- Synapsins and the Synaptic Vesicle Reserve Pool: Floats or Anchors? vol.10, pp.3, 2015, https://doi.org/10.3390/cells10030658
- Rho‐kinase inhibition by fasudil modulates pre‐synaptic vesicle dynamics vol.157, pp.4, 2015, https://doi.org/10.1111/jnc.15274
- Dynamic Foot Stimulations During Short-Term Hindlimb Unloading Prevent Dysregulation of the Neurotransmission in the Hippocampus of Rats vol.41, pp.7, 2021, https://doi.org/10.1007/s10571-020-00922-2