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Complexin 1

complexin I, Complexin, CPX-1
binds the assembled SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) complex; modulates synaptic vesicle exocytosis [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, ACID, Synaptophysin, SNAP-25, V1a
Papers on complexin I
Carboxypeptidase X-1 (CPX-1) is a secreted collagen-binding glycoprotein.
Whitehead et al., Brisbane, Australia. In Biochem Biophys Res Commun, Jan 2016
Carboxypeptidase X-1 (CPX-1) is an atypical member of the carboxypeptidase (CP) family of proteins involved in a variety of physiological and pathological processes.
Phosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity.
Littleton et al., Cambridge, United States. In Neuron, Dec 2015
Here we show that the SNARE fusion clamp Complexin undergoes activity-dependent phosphorylation that alters the basic properties of neurotransmission in Drosophila.
Complexin stabilizes newly primed synaptic vesicles and prevents their premature fusion at the mouse calyx of held synapse.
Taschenberger et al., Göttingen, Germany. In J Neurosci, Jun 2015
We therefore studied consequences of genetic ablation of Cplx1 in the mouse calyx of Held synapse, and discovered a developmentally exacerbating phenotype of reduced spontaneous and evoked transmission but excessive asynchronous release after stimulation, compatible with combined facilitating and clamping functions of Cplx1.
Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo.
Littleton et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2014
Complexin (Cpx) is a SNARE-binding protein that regulates neurotransmission by clamping spontaneous synaptic vesicle fusion in the absence of Ca(2+) influx while promoting evoked release in response to an action potential.
Complexin synchronizes primed vesicle exocytosis and regulates fusion pore dynamics.
Bruns et al., Homburg, Germany. In J Cell Biol, 2014
ComplexinII (CpxII) and SynaptotagminI (SytI) have been implicated in regulating the function of SNARE proteins in exocytosis, but their precise mode of action and potential interplay have remained unknown.
The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.
Montecucco et al., Montevideo, Uruguay. In Cell Mol Life Sci, 2014
To explain these facts and other experimental data, we present here a model for the assembly of the neuroexocytosis apparatus in which Synaptotagmin and Complexin first assist the zippering of the SNARE complex, and then stabilize and clamp an octameric radial assembly of the SNARE complexes.
Differences in human cortical gene expression match the temporal properties of large-scale functional networks.
Mesmoudi et al., Paris, France. In Plos One, 2013
Ionic channels and release-related proteins more expressed in the VSA ring favor temporal precision of fast evoked neural transmission (Sodium channels SCNA1, SCNB1 potassium channel KCNA1, calcium channel CACNA2D2, Synaptotagmin SYT2, Complexin CPLX1, Synaptobrevin VAMP1).
Neurotransmitter release: the last millisecond in the life of a synaptic vesicle.
Südhof, Stanford, United States. In Neuron, 2013
Complexin adaptor proteins assist synaptotagmin by activating and clamping this core fusion machinery.
Complexin controls spontaneous and evoked neurotransmitter release by regulating the timing and properties of synaptotagmin activity.
Littleton et al., Cambridge, United States. In J Neurosci, 2013
Several families of SNARE-binding proteins have evolved to regulate synaptic exocytosis, including Synaptotagmin (SYT) and Complexin (CPX).
SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1.
Söllner et al., Heidelberg, Germany. In J Biol Chem, 2012
Complexin II stalls SNAREpin zippering at a late stage and, hence, contributes to synchronize membrane fusion in a Ca(2+)- and synaptotagmin 1-dependent manner.
Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release.
Söllner et al., Heidelberg, Germany. In Embo J, 2012
Together with synaptotagmin 1, complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2+) concentrations.
A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion.
Rothman et al., New Haven, United States. In Nat Struct Mol Biol, 2011
The crystal structure of complexin bound to a prefusion SNAREpin mimetic shows that the accessory helix extends away from the SNAREpin in an 'open' conformation, binding another SNAREpin and inhibiting its assembly, to clamp fusion.
Complexin cross-links prefusion SNAREs into a zigzag array.
Reinisch et al., New Haven, United States. In Nat Struct Mol Biol, 2011
The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45 degrees and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion.
Use of nanoscale delivery systems to maintain synergistic drug ratios in vivo.
Tardi et al., Vancouver, Canada. In Expert Opin Drug Deliv, 2010
We describe how manipulation of the lipid membrane and internal buffer composition maintains synergistic ratios of irinotecan and floxuridine (CPX-1), daunorubicin and cytarabine (CPX-351) or cisplatin and irinotecan (CPX-571).
A Cdc20-APC ubiquitin signaling pathway regulates presynaptic differentiation.
Bonni et al., Boston, United States. In Science, 2009
The NeuroD2 target gene encoding Complexin II, which acts locally at presynaptic sites, mediated the ability of NeuroD2 to suppress presynaptic differentiation.
Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1.
Abe et al., Japan. In Brain Cell Biol, 2008
Data show direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1.
Regulation of complexin 1 and complexin 2 in the developing human prefrontal cortex.
Jarskog et al., Chapel Hill, United States. In Synapse, 2008
CX1 level increased progressively across development
Sealed with a twist: complexin and the synaptic SNARE complex.
Hanson et al., Saint Louis, United States. In Trends Neurosci, 2002
In the recently solved crystal structure of complexin I bound to the synaptic SNARE complex, complexin binds along the groove between the syntaxin and synaptobrevin coils.
Carboxypeptidases from A to z: implications in embryonic development and Wnt binding.
Fricker et al., New York City, United States. In Cell Mol Life Sci, 2001
Three other members of the metallocarboxypeptidase gene family do not appear to encode active enzymes; these members have been designated CPX-1, CPX-2 and AEBP1/ACLP.
Preferential involvement of excitatory neurons in medial temporal lobe in schizophrenia.
Eastwood et al., Oxford, United Kingdom. In Lancet, 1998
In mice, the presynaptic protein complexin I is a marker of axosomatic (inhibitory) synapses, whereas complexin II is a marker of axodendritic (mainly excitatory) synapses.
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