ArticleProtein science : a publication of the Protein Society2014
Cdk5 phosphorylation of EFhd2 at S74 affects its calcium binding activity.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- EFhd2 co-aggregates with monomeric and filamentous tauFrontiers in neuroscience · 2024Article
- EFhd2 brain interactome reveals its association with different cellular and molecular processes.Journal of neurochemistry · 2021Article
- Association betweenThe Journal of international medical research · 2020Article
- EFhd2 Affects Tau Liquid-Liquid Phase Separation.Frontiers in neuroscience · 2019Article
- EF Hand Domain Family Member D2 Is Required for T Cell Cytotoxicity.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Impact of Swiprosin-1/Efhd2 on Adult Hippocampal Neurogenesis.Stem cell reports · 2018Article
- Physiological and pathophysiological functions of Swiprosin-1/EFhd2 in the nervous system.The Biochemical journal · 2016Review
- EFhd2, a Protein Linked to Alzheimer's Disease and Other Neurological Disorders.Frontiers in neuroscience · 2016Review
- The calcium-binding protein EFhd2 modulates synapse formation in vitro and is linked to human dementia.Journal of neuropathology and experimental neurology · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
EFhd2 is a calcium binding protein, which is highly expressed in the central nervous system and associated with pathological forms of tau proteins in tauopathies. Previous phosphoproteomics studies and bioinformatics analysis suggest that EFhd2 may be phosphorylated. Here, we determine whether Cdk5, a hyperactivated kinase in tauopathies, phosphorylates EFhd2 and influence its known molecular activities. The results indicated that EFhd2 is phosphorylated by brain extract of the transgenic mouse CK-p25, which overexpresses the Cdk5 constitutive activator p25. Consistently, in vitro kinase assays demonstrated that Cdk5, but not GSK3β, directly phosphorylates EFhd2. Biomass, tandem mass spectrometry, and mutagenesis analyses indicated that Cdk5 monophosphorylates EFhd2 at S74, but not the adjacent S76. Furthermore, Cdk5-mediated phosphorylation of EFhd2 affected its calcium binding activity. Finally, a phospho-specific antibody was generated against EFhd2 phosphorylated at S74 and was used to detect this phosphorylation event in postmortem brain tissue from Alzheimer's disease and normal-aging control cases. Results demonstrated that EFhd2 is phosphorylated in vivo at S74. These results imply that EFhd2's physiological and/or pathological function could be regulated by its phosphorylation state.
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