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data define CPLX1 as a PD risk factor and provide functional insights into the role and regulation of blood SNCA levels. The new blood biomarkers of PARK4 in this Turkish family might become useful for PD prediction
Homozygous CPLX1 variants were identified in three patients with severe infantile myoclonic epilepsy and ID.
This study demonstrated that complexin-I influence cognitive function in early and late stages of Alzheimer's disease.
Study showed for the first time that neuro-Behcet's disease and Behcet's disease patients are inclined to display the GG genotype of the CPLX1 rs936551 polymorphism and to exhibit increased CPLX1 expression levels
Collectively these results demonstrate that CPX-1 is a secreted collagen-binding glycoprotein and provide a foundation for future studies investigating the function of CPX-1.
Studies indicate the role of the small regulatory factor complexin in Ca(2 (zeige CA2 Proteine)+)-dependent vesicle fusion and exocytosis.
Together with synaptotagmin 1 (zeige SYT1 Proteine), complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2 (zeige CA2 Proteine)+) concentrations.
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.
The 'central helix' of complexin is anchored to one SNARE (zeige NAPA Proteine) complex, while its 'accessory helix' extends away at ~45 degrees and bridges to a second complex, occupying the vacant v-SNARE (zeige VTI1B Proteine) binding site to inhibit fusion.
description of what may represent a basic principle of the coupling mechanism in SNARE (zeige NAPA Proteine) dependent exocytosis: a reversible clamping protein, complexin, that can freeze the SNAREpin, an assembled fusion-competent intermediate en route to fusion
The response of CPLX1 and Foxp1 levels to SNCA deficiency supports the notion that these factors are regulated by altered physiological function of alpha-synuclein.
In the absence of Cplx1, synaptic vesicles remain unstable and prone to premature fusion.
Cplx 1 and 2 play a role in facilitating vesicle priming, and also lead to the new hypothesis that Cplxs may synchronize vesicle release by promoting coupling between secretory vesicles and calcium channels.
Complexin-1 carboxyl-terminal domain binds lipids through a novel protein motif by targeting complexin-1 to synaptic vesicles.
the ataxia in Cplx1(-/-) mice is likely to be due to pathological changes in both cerebellum and thalamus
This study demonistrated that relatively large C-terminal complexin-1 sequence acts in priming and clamping synaptic exocytosis and demonstrate that the clamping function
The study uncovers an interaction between the complexin-1 N terminus and the SNARE (zeige VTI1B Proteine) complex C terminus, and shows that disrupting this interaction abolishes the facilitatory function of complexins in mouse neurons.
CPX I plays a critical role in beta-cells in the control of the stimulated-exocytosis of insulin (zeige INS Proteine).
Here we propose that complexin binding activates SNARE (zeige VTI1B Proteine) complexes into a metastable state and that Ca(2 (zeige CA2 Proteine)+) binding to synaptotagmin 1 (zeige SYT1 Proteine) triggers fast exocytosis by displacing complexin from metastable SNARE (zeige VTI1B Proteine) complexes.
Its co-localization and interaction with complexin I suggest that dynamin 2 (zeige DNM2 Proteine) may play a role during acrosome formation and/or acrosomal exocytosis.
Proteins encoded by the complexin/synaphin gene family are cytosolic proteins that function in synaptic vesicle exocytosis. These proteins bind syntaxin, part of the SNAP receptor. The protein product of this gene binds to the SNAP receptor complex and disrupts it, allowing transmitter release.
, CPX I
, complexin I
, synaphin 2