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    SYNE2 spectrin repeat containing nuclear envelope protein 2 [ Homo sapiens (human) ]

    Gene ID: 23224, updated on 7-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Mena regulates nesprin-2 to control actin-nuclear lamina associations, trans-nuclear membrane signalling and gene expression.

    Mena regulates nesprin-2 to control actin-nuclear lamina associations, trans-nuclear membrane signalling and gene expression.
    Li Mow Chee F, Beernaert B, Griffith BGC, Loftus AEP, Kumar Y, Wills JC, Lee M, Valli J, Wheeler AP, Armstrong JD, Parsons M, Leigh IM, Proby CM, von Kriegsheim A, Bickmore WA, Frame MC, Byron A., Free PMC Article

    03/28/2023
    Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.

    Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.
    Yi J, Zhao X, Noell CR, Helmer P, Solmaz SR, Vallee RB., Free PMC Article

    03/22/2023
    Silencing of Nesprin-2 inhibits the differentiation of myofibroblasts from fibroblasts induced by mechanical stretch.

    Silencing of Nesprin-2 inhibits the differentiation of myofibroblasts from fibroblasts induced by mechanical stretch.
    Xu Q, Miao Y, Ren J, Sun Y, Li C, Cai X, Wang Z., Free PMC Article

    07/23/2022
    Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.

    Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.
    Lim SM, Cruz VE, Antoku S, Gundersen GG, Schwartz TU., Free PMC Article

    01/15/2022
    The SUN2-nesprin-2 LINC complex and KIF20A function in the Golgi dispersal.

    The SUN2-nesprin-2 LINC complex and KIF20A function in the Golgi dispersal.
    Hieda M, Matsumoto T, Isobe M, Kurono S, Yuka K, Kametaka S, Wang JY, Chi YH, Kameda K, Kimura H, Matsuura N, Matsuura S., Free PMC Article

    12/18/2021
    A novel SYNE2 mutation identified by whole exome sequencing in a Korean family with Emery-Dreifuss muscular dystrophy.

    A novel SYNE2 mutation identified by whole exome sequencing in a Korean family with Emery-Dreifuss muscular dystrophy.
    Lee SJ, Lee S, Choi E, Shin S, Park J.

    02/2/2021
    Nesprin-1-alpha2 associates with kinesin at myotube outer nuclear membranes, but is restricted to neuromuscular junction nuclei in adult muscle.

    Nesprin-1-alpha2 associates with kinesin at myotube outer nuclear membranes, but is restricted to neuromuscular junction nuclei in adult muscle.
    Holt I, Fuller HR, Lam LT, Sewry CA, Shirran SL, Zhang Q, Shanahan CM, Morris GE., Free PMC Article

    11/21/2020
    Results indicate that sperm associated antigen 4 (SPAG4L/SPAG4Lbeta) transcript isoform interacts with spectrin repeat containing nuclear envelope protein 2 (Nesprin2) in the meiotic process.

    SPAG4L/SPAG4Lβ interacts with Nesprin2 to participate in the meiosis of spermatogenesis.
    Li X, Wu Y, Huang L, Yang L, Xing X.

    01/4/2020
    CRISPR/Cas9-mediated knockout of Syne-2 in cell culture led to an overexpression and mislocalization of Pcnt and to ciliogenesis defects. This suggests that the Pcnt-Syne-2 complex is important for ciliogenesis and outer segment formation during retinal development and plays a role in nuclear migration.

    Functional analyses of Pericentrin and Syne-2 interaction in ciliogenesis.
    Falk N, Kessler K, Schramm SF, Boldt K, Becirovic E, Michalakis S, Regus-Leidig H, Noegel AA, Ueffing M, Thiel CT, Roepman R, Brandstätter JH, Gießl A.

    11/30/2019
    Study shows that modulation of matrix pore size or of lamin A expression known to modulate nuclear stiffness directly impinges on levels of MT1-MMP-mediated pericellular collagenolysis by cancer cells. This response requires an intact connection between the nucleus and the centrosome via the linker of nucleoskeleton and cytoskeleton (LINC) complex protein nesprin-2 and dynein adaptor Lis1.

    LINC complex-Lis1 interplay controls MT1-MMP matrix digest-on-demand response for confined tumor cell migration.
    Infante E, Castagnino A, Ferrari R, Monteiro P, Agüera-González S, Paul-Gilloteaux P, Domingues MJ, Maiuri P, Raab M, Shanahan CM, Baffet A, Piel M, Gomes ER, Chavrier P., Free PMC Article

    01/19/2019
    variants of EGFR and SYNE2 play an important role in p21 regulation and are associated with the clinical outcome of HBV-related hepatocellular carcinoma in a TP53-indenpdent manner

    EGFR and SYNE2 are associated with p21 expression and SYNE2 variants predict post-operative clinical outcomes in HBV-related hepatocellular carcinoma.
    Han C, Liao X, Qin W, Yu L, Liu X, Chen G, Liu Z, Lu S, Chen Z, Su H, Zhu G, Lu Z, Liu Z, Qin X, Gui Y, Mo Z, Li L, Peng T., Free PMC Article

    07/7/2018
    The authors identified the nuclear envelope protein nesprin-2 as a binding partner for fascin in a range of cell types in vitro and in vivo. Nesprin-2 interacts with fascin through a direct, F-actin-independent interaction, and this binding is distinct and separable from a role for fascin within filopodia at the cell periphery.

    Fascin Regulates Nuclear Movement and Deformation in Migrating Cells.
    Jayo A, Malboubi M, Antoku S, Chang W, Ortiz-Zapater E, Groen C, Pfisterer K, Tootle T, Charras G, Gundersen GG, Parsons M., Free PMC Article

    07/1/2017
    these data identify N-terminal nesprin-2 variants as novel regulators of beta-catenin signaling.

    N-terminal nesprin-2 variants regulate β-catenin signalling.
    Zhang Q, Minaisah RM, Ferraro E, Li C, Porter LJ, Zhou C, Gao F, Zhang J, Rajgor D, Autore F, Shanahan CM, Warren DT., Free PMC Article

    05/20/2017
    We show that AMPH-1/BIN1 binds to nesprin and actin, as well as to the microtubule-binding protein CLIP170 in both species. We propose that BIN1 has a direct and evolutionarily conserved role in nuclear positioning, altered in myopathies.

    Amphiphysin 2 Orchestrates Nucleus Positioning and Shape by Linking the Nuclear Envelope to the Actin and Microtubule Cytoskeleton.
    D'Alessandro M, Hnia K, Gache V, Koch C, Gavriilidis C, Rodriguez D, Nicot AS, Romero NB, Schwab Y, Gomes E, Labouesse M, Laporte J.

    02/13/2016
    The significance of these shorter isoforms of nesprin, were evaluated.

    Nesprins: tissue-specific expression of epsilon and other short isoforms.
    Duong NT, Morris GE, Lam le T, Zhang Q, Sewry CA, Shanahan CM, Holt I., Free PMC Article

    07/4/2015
    nesprin-1 and nesprin-2 both regulate nuclear and cytoplasmic architecture.

    Nesprin-1 and nesprin-2 regulate endothelial cell shape and migration.
    King SJ, Nowak K, Suryavanshi N, Holt I, Shanahan CM, Ridley AJ.

    04/4/2015
    nesprin-dependent recruitment of kinesin-1 to the nuclear envelope through the interaction of a conserved LEWD motif with kinesin light chain might be a general mechanism for cell-type-specific nuclear positioning during development.

    Nesprins anchor kinesin-1 motors to the nucleus to drive nuclear distribution in muscle cells.
    Wilson MH, Holzbaur EL., Free PMC Article

    02/21/2015
    Each mutation in LMNA has a distinct impact on the Nersprin-2 interaction that substantially explains how distinct mutations in widely expressed genes lead to the formation of phenotypically different diseases.

    Mutations in LMNA modulate the lamin A--Nesprin-2 interaction and cause LINC complex alterations.
    Yang L, Munck M, Swaminathan K, Kapinos LE, Noegel AA, Neumann S., Free PMC Article

    04/12/2014
    High Nesprin-2 expression is associated with colorectal cancer.

    Nonsteroidal anti-inflammatory drug sulindac sulfide suppresses structural protein Nesprin-2 expression in colorectal cancer cells.
    Liggett JL, Choi CK, Donnell RL, Kihm KD, Kim JS, Min KW, Noegel AA, Baek SJ., Free PMC Article

    03/15/2014
    ectopic expression of BRAP2 inhibits nuclear localization of HMG20A and NuMA1, and prevents nuclear envelope accumulation of SYNE2.

    The BRCA1-binding protein BRAP2 can act as a cytoplasmic retention factor for nuclear and nuclear envelope-localizing testicular proteins.
    Davies RG, Wagstaff KM, McLaughlin EA, Loveland KL, Jans DA.

    03/1/2014
    Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds.

    Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds.
    Rajgor D, Mellad JA, Autore F, Zhang Q, Shanahan CM., Free PMC Article

    11/17/2012
    Study presents crystal structures of the human SUN2-KASH1/2 complex, i.e. SUN2 complexed with the C-terminal 29 residues of human Nesprin-1 or -2 (the core of the LINC complex).

    LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins.
    Sosa BA, Rothballer A, Kutay U, Schwartz TU., Free PMC Article

    08/4/2012
    novel isoform, nesprin-2-epsilon, was found to be the major mRNA and protein product of the nesprin-2 gene.

    Nesprin-2 epsilon: a novel nesprin isoform expressed in human ovary and Ntera-2 cells.
    Lam le T, Böhm SV, Roberts RG, Morris GE.

    10/22/2011
    Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development

    Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development.
    Randles KN, Lam le T, Sewry CA, Puckelwartz M, Furling D, Wehnert M, McNally EM, Morris GE., Free PMC Article

    12/11/2010
    Nesprin-2 interacts with {alpha}-catenin and regulates Wnt signaling at the nuclear envelope.

    Nesprin-2 interacts with {alpha}-catenin and regulates Wnt signaling at the nuclear envelope.
    Neumann S, Schneider M, Daugherty RL, Gottardi CJ, Eming SA, Beijer A, Noegel AA, Karakesisoglou I., Free PMC Article

    12/4/2010
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