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    DYNLL1 dynein light chain LC8-type 1 [ Homo sapiens (human) ]

    Gene ID: 8655, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Dynein light chain LC8 alleviates nonalcoholic steatohepatitis by inhibiting NF-kappaB signaling and reducing oxidative stress.

    Dynein light chain LC8 alleviates nonalcoholic steatohepatitis by inhibiting NF-κB signaling and reducing oxidative stress.
    Lee GR, Lee HI, Kim N, Lee J, Kwon M, Kang YH, Song HJ, Yeo CY, Jeong W.

    10/8/2022
    DYNLL1 is hypomethylated and upregulated in a tumor stage- and grade-dependent manner and associated with increased mortality in hepatocellular carcinoma.

    DYNLL1 is hypomethylated and upregulated in a tumor stage- and grade-dependent manner and associated with increased mortality in hepatocellular carcinoma.
    Berkel C, Cacan E.

    02/6/2021
    The multiple associations of the regulatory proteins of the microtubule network could ensure fine tuning in the regulation of the intracellular trafficking process either by the complexation of DYNLL/LC8 with new partners or indirectly by the modulation of the acetylation level of the microtubule network.

    Interactions between two regulatory proteins of microtubule dynamics, HDAC6, TPPP/p25, and the hub protein, DYNLL/LC8.
    Oláh J, Szunyogh S, Szénási T, Szaniszló T, Szabó A, Lehotzky A, Berki T, Nyitray L, Ovádi J.

    03/21/2020
    The data establish LC8 as an important mediator of a subset of 53BP1-dependent DNA double-strand breaks responses.

    LC8/DYNLL1 is a 53BP1 effector and regulates checkpoint activation.
    West KL, Kelliher JL, Xu Z, An L, Reed MR, Eoff RL, Wang J, Huen MSY, Leung JWC., Free PMC Article

    02/29/2020
    identification of recognition motifs for binding partners for the hub protein LC8.

    Systematic identification of recognition motifs for the hub protein LC8.
    Jespersen N, Estelle A, Waugh N, Davey NE, Blikstad C, Ammon YC, Akhmanova A, Ivarsson Y, Hendrix DA, Barbar E., Free PMC Article

    12/21/2019
    DYNLL1 binds directly to MRE11 to limit its end-resection activity; it is inferred that DYNLL1 is an important anti-resection factor that influences genomic stability and responses to DNA-damaging chemotherapy

    DYNLL1 binds to MRE11 to limit DNA end resection in BRCA1-deficient cells.
    He YJ, Meghani K, Caron MC, Yang C, Ronato DA, Bian J, Sharma A, Moore J, Niraj J, Detappe A, Doench JG, Legube G, Root DE, D'Andrea AD, Drané P, De S, Konstantinopoulos PA, Masson JY, Chowdhury D., Free PMC Article

    05/18/2019
    It has been found that APC2 localizes as distinct clusters along microtubule bundles in dendrites, and that this localization is driven by LC8-binding and two separate microtubule-interacting domains.

    APC2 controls dendrite development by promoting microtubule dynamics.
    Kahn OI, Schätzle P, van de Willige D, Tas RP, Lindhout FW, Portegies S, Kapitein LC, Hoogenraad CC., Free PMC Article

    12/22/2018
    High PIN expression is associated with Dilated Hearts.

    Protein Inhibitor of NOS1 Plays a Central Role in the Regulation of NOS1 Activity in Human Dilated Hearts.
    Roselló-Lletí E, Tarazón E, Ortega A, Gil-Cayuela C, Carnicer R, Lago F, González-Juanatey JR, Portolés M, Rivera M., Free PMC Article

    06/30/2018
    An expanded list of LC8 binding partners revealed the evolutionary plasticity of binding partners despite the highly conserved binding interface. In addition, it also highlighted a novel, conserved function of LC8 in the upstream regulation of the Hippo signaling pathway.

    Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.
    Erdős G, Szaniszló T, Pajkos M, Hajdu-Soltész B, Kiss B, Pál G, Nyitray L, Dosztányi Z., Free PMC Article

    01/27/2018
    DLC1 binding to nNOS-calmodulin complex does not affect the electron transport from the reductase to the oxygenase domain.

    The protein inhibitor of nNOS (PIN/DLC1/LC8) binding does not inhibit the NADPH-dependent heme reduction in nNOS, a key step in NO synthesis.
    Parhad SS, Jaiswal D, Ray K, Mazumdar S.

    08/13/2016
    NMR-derived secondary chemical shifts and relaxation properties show that the Chica LC8 binding domain is essentially disordered with a dynamically restricted segment in one linker between motifs.

    The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex.
    Clark S, Nyarko A, Löhr F, Karplus PA, Barbar E., Free PMC Article

    05/14/2016
    Studies indicate that dynein light chain LC8 has been termed an intrinsically disordered proteins (IDPs) dimerization 'hub' protein.

    Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.
    Clark SA, Jespersen N, Woodward C, Barbar E., Free PMC Article

    01/16/2016
    DLC1 binding motif in L is involved in cytoskeleton localization and reorganization, primary transcription regulation by DLC1, and regulation of cellular DLC1 gene expression.

    A Dynein Light Chain 1 Binding Motif in Rabies Virus Polymerase L Protein Plays a Role in Microtubule Reorganization and Viral Primary Transcription.
    Bauer A, Nolden T, Nemitz S, Perlson E, Finke S., Free PMC Article

    11/7/2015
    The dynein light intermediate chain has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins.

    A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region.
    Schroeder CM, Ostrem JM, Hertz NT, Vale RD., Free PMC Article

    07/4/2015
    Authors demonstrate that the interaction between ebola virus VP35 and dynein LC8 is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis.

    Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis.
    Luthra P, Jordan DS, Leung DW, Amarasinghe GK, Basler CF., Free PMC Article

    06/20/2015
    Overall, this study demonstrates the novel interaction between HIV-1 integrase and cellular DYNLL1 proteins and suggests the requirement of this virus-cell interaction for proper uncoating and efficient reverse transcription of HIV-1.

    Human immunodeficiency virus type 1 employs the cellular dynein light chain 1 protein for reverse transcription through interaction with its integrase protein.
    Jayappa KD, Ao Z, Wang X, Mouland AJ, Shekhar S, Yang X, Yao X., Free PMC Article

    05/23/2015
    Structural analysis of LC8 with both Nek9 peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 to LC8 upon phosphorylation on Ser(944) within the Nek9 sequence

    Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.
    Gallego P, Velazquez-Campoy A, Regué L, Roig J, Reverter D., Free PMC Article

    06/29/2013
    Dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis.

    Systematic dissection of dynein regulators in mitosis.
    Raaijmakers JA, Tanenbaum ME, Medema RH., Free PMC Article

    06/15/2013
    Overexpressed human LC8 inhibits mouse osteoclast differentiation by regulating NF-kappaB & MAPK pathways and suppressing RANKL signaling.

    Dynein light chain LC8 inhibits osteoclast differentiation and prevents bone loss in mice.
    Kim H, Hyeon S, Kim H, Yang Y, Huh JY, Park DR, Lee H, Seo DH, Kim HS, Lee SY, Jeong W.

    03/30/2013
    DYNLL1 interacted with a spindle-microtubule-associated adaptor formed by CHICA and HMMR via TQT motifs in CHICA.

    Dynein light chain 1 and a spindle-associated adaptor promote dynein asymmetry and spindle orientation.
    Dunsch AK, Hammond D, Lloyd J, Schermelleh L, Gruneberg U, Barr FA., Free PMC Article

    02/16/2013
    appropriate levels of ternary complex components are critical for dynein-dependent spindle positioning in HeLa cells and C. elegans embryos

    Cortical dynein is critical for proper spindle positioning in human cells.
    Kotak S, Busso C, Gönczy P., Free PMC Article

    02/9/2013
    Cytosolic mfGbeta is recruited to dynein by Nudel and transported to the centrosome for rapid sequestration and degradation.

    Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance.
    Wan Y, Yang Z, Guo J, Zhang Q, Zeng L, Song W, Xiao Y, Zhu X., Free PMC Article

    10/27/2012
    Study found the secretion of calu-1/2-EGFP required microtubule integrity, and that calu-1/2-EGFP-containing vesicles were transported by the motor proteins Kif5b and cytoplasmic dynein.

    The intracellular transport and secretion of calumenin-1/2 in living cells.
    Wang Q, Feng H, Zheng P, Shen B, Chen L, Liu L, Liu X, Hao Q, Wang S, Chen J, Teng J., Free PMC Article

    09/1/2012
    The ASCIZ-DYNLL1 feedback loop represents a novel mechanism for auto-regulation of gene expression, where the gene product directly inhibits the transcriptional activator while bound at its own promoter.

    ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional transcriptional activator and feedback sensor in the regulation of dynein light chain (DYNLL1) expression.
    Jurado S, Conlan LA, Baker EK, Ng JL, Tenis N, Hoch NC, Gleeson K, Smeets M, Izon D, Heierhorst J., Free PMC Article

    03/24/2012
    The study uses thermodynamics and dynamics measurements of LC8 complexes to group LC8 binding partners in two categories: those whose binding is enthalpically driven and those that are entropically favored.

    Conformational dynamics promote binding diversity of dynein light chain LC8.
    Nyarko A, Hall J, Hall A, Hare M, Kremerskothen J, Barbar E.

    01/21/2012
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