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    CPLX1 complexin 1 [ Homo sapiens (human) ]

    Gene ID: 10815, updated on 3-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis.

    Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis.
    Ramakrishnan S, Bera M, Coleman J, Rothman JE, Krishnakumar SS., Free PMC Article

    03/20/2021
    Findings do not support microRNA137 (MIR137) and complexin 1 (CPLX1) conferring susceptibility to schizophrenia in Han Chinese.

    Genetic association analysis of microRNA137 and its target complex 1 with schizophrenia in Han Chinese.
    Lu W, Zhang Y, Fang X, Fan W, Tang W, Cai J, Song L, Zhang C., Free PMC Article

    07/13/2019
    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

    Blood RNA biomarkers in prodromal PARK4 and rapid eye movement sleep behavior disorder show role of complexin 1 loss for risk of Parkinson's disease.
    Lahut S, Gispert S, Ömür Ö, Depboylu C, Seidel K, Domínguez-Bautista JA, Brehm N, Tireli H, Hackmann K, Pirkevi C, Leube B, Ries V, Reim K, Brose N, den Dunnen WF, Johnson M, Wolf Z, Schindewolf M, Schrempf W, Reetz K, Young P, Vadasz D, Frangakis AS, Schröck E, Steinmetz H, Jendrach M, Rüb U, Başak AN, Oertel W, Auburger G., Free PMC Article

    06/23/2018
    Homozygous CPLX1 variants were identified in three patients with severe infantile myoclonic epilepsy and ID.

    Variants in CPLX1 in two families with autosomal-recessive severe infantile myoclonic epilepsy and ID.
    Redler S, Strom TM, Wieland T, Cremer K, Engels H, Distelmaier F, Schaper J, Küchler A, Lemke JR, Jeschke S, Schreyer N, Sticht H, Koch M, Lüdecke HJ, Wieczorek D., Free PMC Article

    09/30/2017
    This study demonstrated that complexin-I influence cognitive function in early and late stages of Alzheimer's disease.

    Presynaptic proteins complexin-I and complexin-II differentially influence cognitive function in early and late stages of Alzheimer's disease.
    Ramos-Miguel A, Sawada K, Jones AA, Thornton AE, Barr AM, Leurgans SE, Schneider JA, Bennett DA, Honer WG., Free PMC Article

    09/23/2017
    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

    Increased complexin-1 and decreased miR-185 expression levels in Behçet's disease with and without neurological involvement.
    Uğurel E, Şehitoğlu E, Tüzün E, Kürtüncü M, Çoban A, Vural B.

    12/17/2016
    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.

    Carboxypeptidase X-1 (CPX-1) is a secreted collagen-binding glycoprotein.
    Kim YH, O'Neill HM, Whitehead JP.

    04/23/2016
    Studies indicate the role of the small regulatory factor complexin in Ca(2+)-dependent vesicle fusion and exocytosis.

    Complexins: small but capable.
    Mohrmann R, Dhara M, Bruns D., Free PMC Article

    04/2/2016
    Data support the the trans insertion model for complexin clamping.

    Re-visiting the trans insertion model for complexin clamping.
    Krishnakumar SS, Li F, Coleman J, Schauder CM, Kümmel D, Pincet F, Rothman JE, Reinisch KM., Free PMC Article

    02/6/2016
    Together with synaptotagmin 1, complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2+) concentrations.

    Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release.
    Malsam J, Parisotto D, Bharat TA, Scheutzow A, Krause JM, Briggs JA, Söllner TH., Free PMC Article

    10/27/2012
    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.

    Complexin cross-links prefusion SNAREs into a zigzag array.
    Kümmel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM., Free PMC Article

    12/3/2011
    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.

    A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion.
    Krishnakumar SS, Radoff DT, Kümmel D, Giraudo CG, Li F, Khandan L, Baguley SW, Coleman J, Reinisch KM, Pincet F, Rothman JE., Free PMC Article

    12/3/2011
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    Human variation in alcohol response is influenced by variation in neuronal signaling genes.
    Joslyn G, Ravindranathan A, Brush G, Schuckit M, White RL.

    04/7/2010
    CX1 level increased progressively across development

    Regulation of complexin 1 and complexin 2 in the developing human prefrontal cortex.
    Salimi K, Glantz LA, Hamer RM, German TT, Gilmore JH, Jarskog LF.

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)

    No association of complexin1 and complexin2 genes with schizophrenia in a Japanese population.
    Kishi T, Ikeda M, Suzuki T, Kitajima T, Yamanouchi Y, Kinoshita Y, Ozaki N, Iwata N.

    03/13/2008
    role in synaptic vesicle exocytosis

    [The mechanism of neurotransmitter release: role of synaphin/complexin in synaptic vesicle exocytosis].
    Abe T.

    01/21/2010
    altered immunoreactivity of this protein in prefrontal cortex in severe mental illness

    Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness.
    Sawada K, Young CE, Barr AM, Longworth K, Takahashi S, Arango V, Mann JJ, Dwork AJ, Falkai P, Phillips AG, Honer WG.

    01/21/2010
    description of what may represent a basic principle of the coupling mechanism in SNARE dependent exocytosis: a reversible clamping protein, complexin, that can freeze the SNAREpin, an assembled fusion-competent intermediate en route to fusion

    A clamping mechanism involved in SNARE-dependent exocytosis.
    Giraudo CG, Eng WS, Melia TJ, Rothman JE.

    01/21/2010
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