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Cited by 161

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration.

Chang, Keun-A, Kim, Hye-Sun, Ha, Tae-Young, Ha, Ji-Won, Shin, Ki Young, Jeong, Yun Ha, Lee, Jean-Pyo, Park, Cheol-Hyoung, Kim, Seonghan, Baik, Tae-Kyoung, Suh, Yoo-Hun·2006·Molecular and Cellular Biology
DOI 10.1128/mcb.02393-05
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Abstract

Amyloid precursor protein (APP) has eight potential phosphorylation sites in its cytoplasmic domain. Recently, it has demonstrated that the constitutive phosphorylation of APP at T668 (APP695 isoform numbering) was observed specifically in the brain. Neuron-specific phosphorylation of APP at T668 is thought to be important for neuronal functions of APP, although its exact physiological significance remains to be clarified. In this study, we show that the phosphorylation of the APP intracellular domain (AICD) at T668 is essential for its binding to Fe65 and its nuclear translocation and affects the resultant neurotoxicity, possibly mediated through the induction of glycogen synthase kinase 3beta and tau phosphorylation by enhancing the formation of a ternary complex with Fe65 and CP2 transcription factor. Taken together, these results suggest that the phosphorylation of AICD at T668 contributes to the neuronal degeneration in Alzheimer's disease (AD) by regulating its translocation into the nucleus and then affects neurodegeneration; therefore, the specific inhibitor of T668 phosphorylation might be the target of AD therapy.

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Crossref · 10.1128/mcb.02393-05

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  • AICD is a signaling molecule that can translocate to the nucleus and regulate expression of manifold genes, some involved in AD pathogenic mechanisms, cytoskeleton dynamics, cell cycle control, or synaptic plasticity.

    “AICD has gained consensus as signaling molecule that can translocate to the nucleus and regulate the expression of manifold genes, some of them involved in AD pathogenic mechanisms (Kim et al., 2003; Chang et al., 2006), but also in cytoskeleton dynamics, cell cycle control or synaptic plasticity.”

    From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Chang et al., 2006

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Metadata

Authors
Chang, K.-A., Kim, H.-S., Ha, T.-Y., Ha, J.-W., Shin, K. Y., Jeong, Y. H., Lee, J.-P., Park, C.-H., Kim, S., Baik, T.-K., & Suh, Y.-H.
Affiliations
  • Department of Pharmacology, College of Medicine, National Creative Research Initiative Center for Alzheimer's Dementia and Neuroscience Research Institute, MRC, Seoul National University, Seoul 110-799, South Korea
  • Department of Pediatrics, School of Medicine, University of California at San Diego, La Jolla, California
  • Department of Anatomy, College of Medicine, Eulji University, Daejeon 301-832, South Korea
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
2006-06-01
Volume
26
Issue
11
Pages
4327-4338
ISSN
1098-5549
DOI
10.1128/mcb.02393-05
Cited by
161
References
3
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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