U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    CAND1 cullin associated and neddylation dissociated 1 [ Homo sapiens (human) ]

    Gene ID: 55832, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    ASCC3 promotes the immunosuppression and progression of non-small cell lung cancer by impairing the type I interferon response via CAND1-mediated ubiquitination inhibition of STAT3.

    ASCC3 promotes the immunosuppression and progression of non-small cell lung cancer by impairing the type I interferon response via CAND1-mediated ubiquitination inhibition of STAT3.
    Ao YQ, Gao J, Jin C, Wang S, Zhang LC, Deng J, Chen ZW, Wang HK, Jiang JH, Ding JY., Free PMC Article

    01/4/2024
    Structural and mechanistic insights into the CAND1-mediated SCF substrate receptor exchange.

    Structural and mechanistic insights into the CAND1-mediated SCF substrate receptor exchange.
    Shaaban M, Clapperton JA, Ding S, Kunzelmann S, Mäeots ME, Maslen SL, Skehel JM, Enchev RI.

    07/12/2023
    Systemwide disassembly and assembly of SCF ubiquitin ligase complexes.

    Systemwide disassembly and assembly of SCF ubiquitin ligase complexes.
    Baek K, Scott DC, Henneberg LT, King MT, Mann M, Schulman BA., Free PMC Article

    05/3/2023
    Cullin-associated and neddylation-dissociated 1 protein (CAND1) governs cardiac hypertrophy and heart failure partially through regulating calcineurin degradation.

    Cullin-associated and neddylation-dissociated 1 protein (CAND1) governs cardiac hypertrophy and heart failure partially through regulating calcineurin degradation.
    Li X, Zhang Y, Zhao Y, Zhou Y, Han Q, Yang Y, Zhang L, Shi L, Jin X, Zhang R, Gao H, Xue G, Li D, Zhang ZR, Lu Y, Yang B, Pan Z.

    08/13/2022
    CAND1 regulates lunapark for the proper tubular network of the endoplasmic reticulum.

    CAND1 regulates lunapark for the proper tubular network of the endoplasmic reticulum.
    Kajiho H, Yamamoto Y, Sakisaka T., Free PMC Article

    11/21/2020
    miR-33a and CAND1 played an important role in lung cancer proliferation and cell migration

    miR-33a inhibits cell proliferation and invasion by targeting CAND1 in lung cancer.
    Kang M, Li Y, Zhao Y, He S, Shi J.

    09/1/2018
    describe the identification of the structural determinants responsible for the CA IX/CAND1 interaction

    Disclosing the Interaction of Carbonic Anhydrase IX with Cullin-Associated NEDD8-Dissociated Protein 1 by Molecular Modeling and Integrated Binding Measurements.
    Buonanno M, Langella E, Zambrano N, Succoio M, Sasso E, Alterio V, Di Fiore A, Sandomenico A, Supuran CT, Scaloni A, Monti SM, De Simone G.

    09/23/2017
    Data show that the differentiation of LiSa-2 preadipocytes is associated with an increase of cullin-associated and neddylation-dissociated 1 (CAND1), COP9 signalosome (CSN), neddylated cullin 3 (Cul3) and the BTB protein Keap1.

    CAND1 exchange factor promotes Keap1 integration into cullin 3-RING ubiquitin ligase during adipogenesis.
    Dubiel D, Ordemann J, Pratschke J, Dubiel W, Naumann M.

    05/21/2016
    The Epstein-Barr virus protein BPLF1, is targeted to cullin-RING ubiquitin ligases (CRLs) via the interaction of the conserved helix-2 with helix-23 of cullins, at a site involved in electrostatic interaction with CAND1.

    Herpes virus deneddylases interrupt the cullin-RING ligase neddylation cycle by inhibiting the binding of CAND1.
    Gastaldello S, Callegari S, Coppotelli G, Hildebrand S, Song M, Masucci MG.

    09/28/2013
    We demonstrate that the accumulation of p27 is associated with an increase of CAND1 and a decrease of Skp2 during adipogenesis of human LiSa-2 preadipocytes. CAND1 knockdown reduces p27 and blocks adipogenesis.

    CAND1-dependent control of cullin 1-RING Ub ligases is essential for adipogenesis.
    Dubiel D, Gierisch ME, Huang X, Dubiel W, Naumann M.

    06/22/2013
    Study shows that Cand1 can unambiguously stimulate SCF activity in vitro by enabling an F box protein-Skp1 complex to access Cul1 that was previously occupied by a different F box protein-Skp1 complex, and that Cand1 promotes assembly in vivo of new F box proteins with pre-existing Cul1 molecules.

    Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.
    Pierce NW, Lee JE, Liu X, Sweredoski MJ, Graham RL, Larimore EA, Rome M, Zheng N, Clurman BE, Hess S, Shan SO, Deshaies RJ., Free PMC Article

    06/1/2013
    CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer.

    CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer.
    Korzeniewski N, Hohenfellner M, Duensing S., Free PMC Article

    02/2/2013
    A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.

    Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
    Martins-de-Souza D, Guest PC, Mann DM, Roeber S, Rahmoune H, Bauder C, Kretzschmar H, Volk B, Baborie A, Bahn S.

    04/26/2012
    COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.

    COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.
    Mao X, Gluck N, Chen B, Starokadomskyy P, Li H, Maine GN, Burstein E., Free PMC Article

    11/26/2011
    CAND1 does not function by sequestering cullins in vivo to prevent substrate receptor autoubiquitination and is likely to regulate cullin RING ligase activity via alternative mechanisms

    Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.
    Chua YS, Boh BK, Ponyeam W, Hagen T., Free PMC Article

    08/6/2011
    miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.

    miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.
    Murata T, Takayama K, Katayama S, Urano T, Horie-Inoue K, Ikeda K, Takahashi S, Kawazu C, Hasegawa A, Ouchi Y, Homma Y, Hayashizaki Y, Inoue S.

    02/26/2011
    SCCRO recruits Ubc12 approximately NEDD8 to the CAND1-Cul1-ROC1 complex but that this is not sufficient to dissociate or overcome the inhibitory effects of CAND1 on cullin neddylation

    SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation.
    Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B., Free PMC Article

    01/21/2010
    TIP120A functions as a negative regulator of SCF E3 ubiquitin ligases and may modulate other cullin ligases in a similar fashion.

    TIP120A associates with cullins and modulates ubiquitin ligase activity.
    Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB.

    01/21/2010
    CAND1 & COP9 signalosome (CSN), major deneddylase of cullins, bind to unneddylated CUL1 in mutually exclusive way. Suppression of CAND1 expression by siRNA enhanced interaction between CUL1 & CSN, suggesting that CAND1 inhibited binding of CSN to CUL1.

    CAND1 enhances deneddylation of CUL1 by COP9 signalosome.
    Min KW, Kwon MJ, Park HS, Park Y, Yoon SK, Yoon JB.

    01/21/2010
    binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex

    CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.
    Zheng J, Yang X, Harrell JM, Ryzhikov S, Shim EH, Lykke-Andersen K, Wei N, Sun H, Kobayashi R, Zhang H.

    01/21/2010
    selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation

    NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.
    Liu J, Furukawa M, Matsumoto T, Xiong Y.

    01/21/2010
    firstprevious page of 1 nextlast