| These data demonstrate a role for FE65 proteins at central and peripheral synapses. | FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.
Strecker P, Ludewig S, Rust M, Mundinger TA, Görlich A, Krächan EG, Mehrfeld C, Herz J, Korte M, Guénette SY, Kins S., Free PMC Article | 03/31/2018 |
| 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 |
| results provide strong evidence that Fe65 plays a role in DNA damage response and cell viability by epigenomic regulation of specific transcriptional programs activated upon genotoxic stress. | An epigenomic role of Fe65 in the cellular response to DNA damage.
Ryu S, Teles F, Minopoli G, Russo T, Rosenfeld MG, Suh Y., Free PMC Article | 10/31/2015 |
| Findings show that amyloid precursor protein-binding proteins FE65 and FE65L1 are essential for the maintenance of lens transparency. | FE65 and FE65L1 amyloid precursor protein-binding protein compound null mice display adult-onset cataract and muscle weakness.
Suh J, Moncaster JA, Wang L, Hafeez I, Herz J, Tanzi RE, Goldstein LE, Guénette SY., Free PMC Article | 08/29/2015 |
| our data suggest that FE65 serves as a link between VLDLR and APP | FE65 as a link between VLDLR and APP to regulate their trafficking and processing.
Dumanis SB, Chamberlain KA, Jin Sohn Y, Jin Lee Y, Guénette SY, Suzuki T, Mathews PM, Pak DTs, Rebeck GW, Suh YH, Park HS, Hoe HS., Free PMC Article | 10/27/2012 |
| FE65 small interfering RNA does not influence Rac1 expression or its activity, although it acts as an adaptor protein with several protein-interaction domains. | Functional and molecular interactions between Rac1 and FE65.
Wang PL, Niidome T, Kume T, Akaike A, Kihara T, Sugimoto H. | 06/9/2012 |
| 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 unique role for the 97 kDa isoform in controlling GnRH-1 neurogenesis that is not redundant with the 60 kDa isoform of FE65. | A role for FE65 in controlling GnRH-1 neurogenesis.
Forni PE, Fornaro M, Guénette S, Wray S., Free PMC Article | 02/26/2011 |
| Results confirm that megalin interacts with APP and FE65, suggesting that these three proteins form a tripartite complex. | Megalin interacts with APP and the intracellular adapter protein FE65 in neurons.
Alvira-Botero X, Pérez-Gonzalez R, Spuch C, Vargas T, Antequera D, Garzón M, Bermejo-Pareja F, Carro E. | 01/22/2011 |
| Data show that the carboxyl-terminal half of FE65, which contains the PI2 domain, failed to stabilize p53, suggesting that the amino-terminal half of the protein plays an important role in the stabilization of p53 in osmotically stressed cells. | Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells.
Kawai T, Nakaya T, Suzuki T. | 05/10/2010 |
| These results demonstrate novel roles of FE65 in synaptic plasticity, acquisition, and retention for certain forms of memory formation. | The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation.
Wang Y, Zhang M, Moon C, Hu Q, Wang B, Martin G, Sun Z, Wang H. | 01/21/2010 |
| the translocation of FE65 to the nuclear matrix, along with the formation of nuclear patches, is required for the stabilization of p53 by its suppression of the proteasome degradation pathway. | Metabolic stabilization of p53 by FE65 in the nuclear matrix of osmotically stressed cells.
Nakaya T, Kawai T, Suzuki T. | 01/21/2010 |
| Fe65 and its interaction with APP play an important role in the response to DNA damage by assisting the recruitment of Tip60-TRRAP to DNA damage sites. | Fe65 is required for Tip60-directed histone H4 acetylation at DNA strand breaks.
Stante M, Minopoli G, Passaro F, Raia M, Vecchio LD, Russo T., Free PMC Article | 01/21/2010 |
| observed similar up-regulation of Nme1 and Nme2 genes, both at the transcript and the protein levels, in the brain of Fe65 knock-out mice, thus highlighting the occurrence of evolutionary conserved mechanisms of Nme expression in nematodes and mammals | A differential proteomic approach reveals an evolutionary conserved regulation of Nme proteins by Fe65 in C. elegans and mouse.
Napolitano F, D'Angelo F, Bimonte M, Perrina V, D'Ambrosio C, Scaloni A, Russo T, Zambrano N. | 01/21/2010 |
| APP-regulated FE65 plays an important role in the early stress response of cells and that FE65 deregulated from APP induces apoptosis. | Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells.
Nakaya T, Kawai T, Suzuki T. | 01/21/2010 |
| a TAG1-APP signalling pathway negatively modulates neurogenesis through Fe65 | A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis.
Ma QH, Futagawa T, Yang WL, Jiang XD, Zeng L, Takeda Y, Xu RX, Bagnard D, Schachner M, Furley AJ, Karagogeos D, Watanabe K, Dawe GS, Xiao ZC. | 01/21/2010 |
| Fe65 regulation of APP proteolysis may be integrally associated with its nuclear signaling function, as all antecedent proteolytic steps prior to release of Fe65 from the membrane are fostered by the APP-Fe65 interaction | Fe65 stimulates proteolytic liberation of the beta-amyloid precursor protein intracellular domain.
Wiley JC, Smith EA, Hudson MP, Ladiges WC, Bothwell M. | 01/21/2010 |
| p65FE65 may be an intracellular mediator in a signaling cascade regulating alpha-secretion of APP | Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPalpha pathway in primates.
Hu Q, Wang L, Yang Z, Cool BH, Zitnik G, Martin GM. | 01/21/2010 |
| Notch1 intracellular domain plays the role of a negative regulator in AICD signaling via the disruption of the AICD-Fe65-Tip60 trimeric complex. | Notch1 intracellular domain suppresses APP intracellular domain-Tip60-Fe65 complex mediated signaling through physical interaction.
Kim SY, Kim MY, Mo JS, Park HS. | 01/21/2010 |
| a complex including APP, FE65 and an additional protein is involved in neurite outgrowth at early stages of neuronal development | A macromolecular complex involving the amyloid precursor protein (APP) and the cytosolic adapter FE65 is a negative regulator of axon branching.
Ikin AF, Sabo SL, Lanier LM, Buxbaum JD., Free PMC Article | 01/21/2010 |
| These studies suggest an important and novel function of FE65 in learning and memory. | Isoform-specific knockout of FE65 leads to impaired learning and memory.
Wang B, Hu Q, Hearn MG, Shimizu K, Ware CB, Liggitt DH, Jin LW, Cool BH, Storm DR, Martin GM. | 01/21/2010 |
| Targeted deletion of two members of the FE65 family of adaptor proteins, FE65 and FE65L1, results in cortical dysplasia and suggests that FE65 proteins are involved in basement membrane assembly. | Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development.
Guénette S, Chang Y, Hiesberger T, Richardson JA, Eckman CB, Eckman EA, Hammer RE, Herz J., Free PMC Article | 01/21/2010 |
| Fe65 plays an essential role in the response of the cells to DNA damage | Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage.
Minopoli G, Stante M, Napolitano F, Telese F, Aloia L, De Felice M, Di Lauro R, Pacelli R, Brunetti A, Zambrano N, Russo T. | 01/21/2010 |
| The areas of highest Fe65 expression included the hippocampus, in which the earliest abnormalities of Alzheimer's disease are detectable. Fe65 also occurred in the cerebellum, thalamus and some brain stem nuclei. Fe65 occurred in hippocampal astrocytes. | Expression of the Fe65 adapter protein in adult and developing mouse brain.
Kesavapany S, Banner SJ, Lau KF, Shaw CE, Miller CC, Cooper JD, McLoughlin DM. | 01/21/2010 |
| phosphorylation of APP(amyloid beta-protein precursor) modulates FE65-dependent gene transactivation through the regulation of FE65 intracellular localization. | Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD.
Nakaya T, Suzuki T. | 01/21/2010 |