Function
Synapsins (SYN) are neuronal phosphoproteins which modulate neurotransmitter release at the pre-synaptic terminal by reversibly tethering synaptic vescicles to the actin cytoskeleton[1].
- Synapsin 1 is involved in synapse formation[2].
- Synapsin 2 is involved in axon formation.
- Synapsin 3 is involved in regulation of dopaminergic neurotransmission[3].
Structural highlights
The 3D structure of the rat synapsin 1 complex with ATP shows the catalytically essential multifunctional loop surrounding the ATP which makes both and with the protein[4]. Water molecules are shown as red spheres.
3D structures of synapsin
Updated on 04-May-2025
{{#tree:id=OrganizedByTopic|openlevels=0|
- 1auv - bSYN1A C-terminal 110-421 - bovine
- 1aux - bSYN1A C-terminal + ATPgS
- 1pk8, 1px2 - rSYN1 + ATP - rat
- 1i7n - rSYN2 C-terminal
- 1i7l - rSYN2 C-terminal + ATP
- 2p0a - hSYN3 actin-binding+synaptic vescicle binding domains 76-417 + AMPPNP - human
}}
References
- ↑ Cesca F, Baldelli P, Valtorta F, Benfenati F. The synapsins: key actors of synapse function and plasticity. Prog Neurobiol. 2010 Aug;91(4):313-48. doi: 10.1016/j.pneurobio.2010.04.006. Epub, 2010 May 10. PMID:20438797 doi:http://dx.doi.org/10.1016/j.pneurobio.2010.04.006
- ↑ Ferreira A, Chin LS, Li L, Lanier LM, Kosik KS, Greengard P. Distinct roles of synapsin I and synapsin II during neuronal development. Mol Med. 1998 Jan;4(1):22-8 PMID:9513186
- ↑ Porton B, Wetsel WC, Kao HT. Synapsin III: role in neuronal plasticity and disease. Semin Cell Dev Biol. 2011 Jun;22(4):416-24. PMID:21827867 doi:10.1016/j.semcdb.2011.07.007
- ↑ Brautigam CA, Chelliah Y, Deisenhofer J. Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I. J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264 doi:10.1074/jbc.M312015200