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    APBB1 amyloid beta precursor protein binding family B member 1 [ Homo sapiens (human) ]

    Gene ID: 322, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Alpha-secretase dependent nuclear localization of the amyloid-beta precursor protein-binding protein Fe65 promotes DNA repair.

    Alpha-secretase dependent nuclear localization of the amyloid-β precursor protein-binding protein Fe65 promotes DNA repair.
    Revol RS, Koistinen NA, Menon PK, Chicote-Gonzàlez A, Iverfeldt K, Ström AL.

    12/6/2023
    Abeta40 Promotes the Osteoblastic Differentiation of Aortic Valve Interstitial Cells through the RAGE Pathway.

    Aβ40 Promotes the Osteoblastic Differentiation of Aortic Valve Interstitial Cells through the RAGE Pathway.
    Wang B, Lin HQ, Li F, Mao ZF, Dong NG.

    07/31/2021
    ARF6-Rac1 signaling-mediated neurite outgrowth is potentiated by the neuronal adaptor FE65 through orchestrating ARF6 and ELMO1.

    ARF6-Rac1 signaling-mediated neurite outgrowth is potentiated by the neuronal adaptor FE65 through orchestrating ARF6 and ELMO1.
    Chan WWR, Li W, Chang RCC, Lau KF.

    04/24/2021
    The findings reveal a novel mechanism whereby GSK3beta stimulates amyloidogenic processing of APP by phosphorylation of FE65 at threonine 579.

    Phosphorylation of FE65 at threonine 579 by GSK3β stimulates amyloid precursor protein processing.
    Lee YS, Chow WNV, Lau KF., Free PMC Article

    06/29/2019
    FE65 is found to activate ELMO1 by diminishing ELMO1 intramolecular autoinhibitory interaction and to promote the targeting of ELMO1 to the plasma membrane, where Rac1 is activated. We also show that FE65, ELMO1, and DOCK180 form a tripartite complex

    Neuronal adaptor FE65 stimulates Rac1-mediated neurite outgrowth by recruiting and activating ELMO1.
    Li W, Tam KMV, Chan WWR, Koon AC, Ngo JCK, Chan HYE, Lau KF., Free PMC Article

    01/12/2019
    Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-beta precursor protein, APP. Here, the subcellular localization was further investigated using TAP-tagged Fe65 constructs expressed in human neuroblastoma cells. Our results indicate that PTB2 rather than the WW domain is important for the nuclear localization of Fe65.

    Nuclear localization of amyloid-β precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis.
    Koistinen NA, Edlund AK, Menon PK, Ivanova EV, Bacanu S, Iverfeldt K., Free PMC Article

    08/26/2017
    Fe65 Ser289 phosphorylation did not affect the transcriptional activity of the Fe65-APP complex, in contrast to the previously described Ser228 site.

    Fe65 Is Phosphorylated on Ser289 after UV-Induced DNA Damage.
    Langlands H, Blain PG, Jowsey PA., Free PMC Article

    07/15/2017
    Our findings imply that APBB1 plays an important role in the maintenance of EMT-associated CSC-like properties and gamma-radiation resistance via activation of IGF1Rbeta/AKT/GSK3beta pathway in lung cancer cells, highlighting APBB1 as a potential target for therapeutic cancer treatment.

    APBB1 reinforces cancer stem cell and epithelial-to-mesenchymal transition by regulating the IGF1R signaling pathway in non-small-cell lung cancer cells.
    Lee JH, Kim JY, Kim SY, Choi SI, Kim KC, Cho EW, Kim IG.

    06/3/2017
    Targeted enhancement of the signaling through the Fe65-cortactin pathway, by either HDAC6 inhibition or Tip60 activation, may lead to the development of new therapeutic drugs that are effective for patients with metastatic breast cancers.

    Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation.
    Sun Y, Sun J, Lungchukiet P, Quarni W, Yang S, Zhang X, Bai W., Free PMC Article

    08/6/2016
    Jagged1 is a novel binding partner of Fe65, and Fe65 may act as a novel effector of Jagged1 signaling.

    Fe65 negatively regulates Jagged1 signaling by decreasing Jagged1 protein stability through the E3 ligase Neuralized-like 1.
    Lee HJ, Yoon JH, Ahn JS, Jo EH, Kim MY, Lee YC, Kim JW, Ann EJ, Park HS.

    12/19/2015
    FE65 influences APP degradation via the proteasome, and phosphorylation of FE65 Ser(610) by SGK1 regulates binding of FE65 to APP, APP turnover and processing.

    Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing.
    Chow WN, Ngo JC, Li W, Chen YW, Tam KM, Chan HY, Miller CC, Lau KF., Free PMC Article

    11/21/2015
    A novel phosphorylation site was identified within Fe65 which mediates gene transcription.

    Fe65 Ser228 is phosphorylated by ATM/ATR and inhibits Fe65-APP-mediated gene transcription.
    Jowsey PA, Blain PG.

    04/11/2015
    The SV2A/FE65 interaction might play a role in synaptic signal transduction.

    Amyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain.
    Nensa FM, Neumann MH, Schrötter A, Przyborski A, Mastalski T, Susdalzew S, Looβe C, Helling S, El Magraoui F, Erdmann R, Meyer HE, Uszkoreit J, Eisenacher M, Suh J, Guénette SY, Röhner N, Kögel D, Theiss C, Marcus K, Müller T., Free PMC Article

    10/11/2014
    Data indicate that Fe65 is a positive estrogen receptor alpha (ERalpha) transcriptional regulator.

    A novel function of the Fe65 neuronal adaptor in estrogen receptor action in breast cancer cells.
    Sun Y, Kasiappan R, Tang J, Webb PL, Quarni W, Zhang X, Bai W., Free PMC Article

    08/9/2014
    FE65 interactions with BLM and MCM proteins may contribute to the neuronal cell cycle re-entry observed in brains affected by Alzheimer's disease.

    FE65 regulates and interacts with the Bloom syndrome protein in dynamic nuclear spheres - potential relevance to Alzheimer's disease.
    Schrötter A, Mastalski T, Nensa FM, Neumann M, Loosse C, Pfeiffer K, Magraoui FE, Platta HW, Erdmann R, Theiss C, Uszkoreit J, Eisenacher M, Meyer HE, Marcus K, Müller T.

    11/16/2013
    A ternary complex consisting of AICD, FE65, and TIP60 down-regulates Stathmin1.

    A ternary complex consisting of AICD, FE65, and TIP60 down-regulates Stathmin1.
    Müller T, Schrötter A, Loosse C, Pfeiffer K, Theiss C, Kauth M, Meyer HE, Marcus K.

    03/23/2013
    Both amyloid-beta precursor protein and Fe65 are co-localized in model Hirano bodies associated with Alzheimer's disease.

    Association of AICD and Fe65 with Hirano bodies reduces transcriptional activation and initiation of apoptosis.
    Ha S, Furukawa R, Fechheimer M., Free PMC Article

    08/11/2012
    Fe65 carries out different functions depending on its location in the regulation of Notch1 signaling.

    Dual regulation of notch1 signaling pathway by adaptor protein fe65.
    Kim MY, Mo JS, Ann EJ, Yoon JH, Park HS., Free PMC Article

    04/21/2012
    A novel FE65 isoform and the regulation of the splicing events leading to its production may contribute to elucidating neuronal specific roles of FE65 and its contribution to Alzheimer's disease pathology.

    Identification and characterization of a neuronal enriched novel transcript encoding the previously described p60Fe65 isoform.
    Domingues SC, Henriques AG, Fardilha M, da Cruz E Silva EF, da Cruz E Silva OA.

    01/14/2012
    Phosphorylation of LRP1 regulates the interaction with Fe65.

    Phosphorylation of LRP1 regulates the interaction with Fe65.
    Klug W, Dietl A, Simon B, Sinning I, Wild K.

    12/3/2011
    Fe65 binds preferentially to low-density lipoprotein receptor-related protein (LRP) carboxyl terminus when phosphorylated at tyrosine-4507 and in complex with amyloid precursor protein (APP).

    Protein interactions among Fe65, the low-density lipoprotein receptor-related protein, and the amyloid precursor protein.
    Mulvihill MM, Guttman M, Komives EA., Free PMC Article

    10/15/2011
    Fe65 and Dab1 compete for binding to APP. Dab1 significantly decreased the amount of APP bound to LRP and the level of secreted APP and APP-CTF in LRP expressing cells

    Dab1 binds to Fe65 and diminishes the effect of Fe65 or LRP1 on APP processing.
    Kwon OY, Hwang K, Kim JA, Kim K, Kwon IC, Song HK, Jeon H.

    01/29/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    reduced levels of Sp1 resulted in downregulation of endogenous FE65 mRNA and protein

    Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1.
    Yu HT, Chan WW, Chai KH, Lee CW, Chang RC, Yu MS, McLoughlin DM, Miller CC, Lau KF.

    08/16/2010
    The data of this demonstrated that the induction of AICD/Fe65 or transgelin significantly alters actin dynamics and mitochondrial function in neuronal cells

    The amyloid precursor protein intracellular domain(AICD) disrupts actin dynamics and mitochondrial bioenergetics.
    Ward MW, Concannon CG, Whyte J, Walsh CM, Corley B, Prehn JH.

    05/3/2010
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