{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tiwari SS"],"funding":["Medical Research Council"],"pagination":["2751-2765"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5035822"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["139(Pt 10)"],"pubmed_abstract":["Characteristic features of Alzheimer's disease are memory loss, plaques resulting from abnormal processing of amyloid precursor protein (APP), and presence of neurofibrillary tangles and dystrophic neurites containing hyperphosphorylated tau. Currently, it is not known what links these abnormalities together. Cytoplasmic FMR1 interacting protein 2 (CYFIP2) has been suggested to regulate mRNA translation at synapses and this may include local synthesis of APP and alpha-calcium/calmodulin-dependent kinase II, a kinase that can phosphorylate tau. Further, CYFIP2 is part of the Wiskott-Aldrich syndrome protein-family verprolin-homologous protein complex, which has been implicated in actin polymerization at synapses, a process thought to be required for memory formation. Our previous studies on"],"journal":["Brain : a journal of neurology"],"pubmed_title":["Alzheimer-related decrease in CYFIP2 links amyloid production to tau hyperphosphorylation and memory loss."],"pmcid":["PMC5035822"],"funding_grant_id":["MR/L016397/1","1523477","G1100695"],"pubmed_authors":["Ghosh A","Aziz W","Hortobagyi T","Noble W","Golash V","Tiwari SS","Troakes C","Daoud J","Giese KP","Mizuno K"],"additional_accession":[]},"is_claimable":false,"name":"Alzheimer-related decrease in CYFIP2 links amyloid production to tau hyperphosphorylation and memory loss.","description":"Characteristic features of Alzheimer's disease are memory loss, plaques resulting from abnormal processing of amyloid precursor protein (APP), and presence of neurofibrillary tangles and dystrophic neurites containing hyperphosphorylated tau. Currently, it is not known what links these abnormalities together. Cytoplasmic FMR1 interacting protein 2 (CYFIP2) has been suggested to regulate mRNA translation at synapses and this may include local synthesis of APP and alpha-calcium/calmodulin-dependent kinase II, a kinase that can phosphorylate tau. Further, CYFIP2 is part of the Wiskott-Aldrich syndrome protein-family verprolin-homologous protein complex, which has been implicated in actin polymerization at synapses, a process thought to be required for memory formation. Our previous studies on","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Oct","modification":"2025-04-21T19:20:24.729Z","creation":"2019-03-26T23:05:30Z"},"accession":"S-EPMC5035822","cross_references":{"pubmed":["27524794"],"doi":["10.1093/brain/aww205"]}}