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Human Complexin 1 Protein expressed in Escherichia coli (E. coli) - ABIN666720
Giraudo, Eng, Melia, Rothman: A clamping mechanism involved in SNARE-dependent exocytosis. in Science (New York, N.Y.) 2006
Show all 3 references for ABIN666720
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 (show CA2 Proteins)+)-dependent vesicle fusion and exocytosis.
Together with synaptotagmin 1 (show SYT1 Proteins), complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2 (show CA2 Proteins)+) 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 (show NAPA Proteins) complex, while its 'accessory helix' extends away at ~45 degrees and bridges to a second complex, occupying the vacant v-SNARE (show VTI1B Proteins) binding site to inhibit fusion.
description of what may represent a basic principle of the coupling mechanism in SNARE (show NAPA Proteins) 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 (show USP14 Proteins) 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 (show VTI1B Proteins) 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 (show INS Proteins).
Here we propose that complexin binding activates SNARE (show VTI1B Proteins) complexes into a metastable state and that Ca(2 (show CA2 Proteins)+) binding to synaptotagmin 1 (show SYT1 Proteins) triggers fast exocytosis by displacing complexin from metastable SNARE (show VTI1B Proteins) complexes.
Its co-localization and interaction with complexin I suggest that dynamin 2 (show DNM2 Proteins) 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