Cited by 149Alzheimer's disease research and treatmentsCalcium signaling and nucleotide metabolismSphingolipid Metabolism and Signaling

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Presenilin mutations linked to familial Alzheimer's disease cause an imbalance in phosphatidylinositol 4,5-bisphosphate metabolism

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Landman, Natalie, Jeong, Soon Youn, Shin, Sun Young, Voronov, Sergey V., Serban, Geo, Kang, Min Suk, Park, Myung Kyu, Di Paolo, Gilbert, Chung, Sungkwon, Kim, Tae-Wan·2006·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0604954103PMC PMC1748258

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Abstract

Phosphatidylinositol 4,5-bisphosphate (PIP 2 ) is an important cellular effector whose functions include the regulation of ion channels and membrane trafficking. Aberrant PIP 2 metabolism has also been implicated in a variety of human disease states, e.g., cancer and diabetes. Here we report that familial Alzheimer's disease (FAD)-associated presenilin mutations cause an imbalance in PIP 2 metabolism. We find that the transient receptor potential melastatin 7 (TRPM7)-associated Mg 2+ -inhibited cation (MIC) channel underlies ion channel dysfunction in presenilin FAD mutant cells, and the observed channel deficits are restored by the addition of PIP 2 , a known regulator of the MIC/TRPM7 channel. Lipid analyses show that PIP 2 turnover is selectively affected in FAD mutant presenilin cells. We also find that modulation of cellular PIP 2 closely correlates with 42-residue amyloid β-peptide (Aβ42) levels. Our data suggest that PIP 2 imbalance may contribute to Alzheimer's disease pathogenesis by affecting multiple cellular pathways, such as the generation of toxic Aβ42 as well as the activity of the MIC/TRPM7 channel, which has been linked to other neurodegenerative conditions. Thus, our study suggests that brain-specific modulation of PIP 2 may offer a therapeutic approach in Alzheimer's disease.

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Authors: Landman, N., Jeong, S. Y., Shin, S. Y., Voronov, S. V., Serban, G., Kang, M. S., Park, M. K., Di Paolo, G., Chung, S., & Kim, T.-W.
Affiliations: Columbia University Irving Medical Center (US)
Sungkyunkwan University (KR)
Department of Pathology, and
ORCID: Shin, Sun Young
Chung, Sungkwon
Kim, Tae-Wan
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2006-12-19
Volume: 103
Issue: 51
Pages: 19524-19529
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0604954103
PMC: PMC1748258
OpenAlex: W2047442659
Cited by: 149
References: 50
Citations by year: 2026: 7 · 2025: 7 · 2024: 5 · 2023: 10 · 2022: 6 · 2021: 1 · 2020: 12 · 2019: 6 · 2018: 3 · 2017: 8 · 2016: 5 · 2015: 8 · 2014: 9 · 2013: 14 · 2012: 13
FWCI: 4.43
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Ellison Medical Foundation
National Institutes of Health
Samsung
National Institute of Neurological Disorders and Stroke (R01NS043467, F31NS051186, NS43467, NS51186)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD047733, R21HD047733)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords: presenilin mutations, familial Alzheimer's disease, phosphatidylinositol 4,5-bisphosphate, TRPM7, ion channel dysfunction, amyloid-beta 42, lipid turnover, Alzheimer's disease pathogenesis, therapeutic target
MeSH terms: Alzheimer Disease, Cell Line, Electrophysiology, Humans, Mutation, Phosphorylation, Blotting, Western, Amyloid beta-Peptides, Protein Serine-Threonine Kinases, Phosphotransferases (Alcohol Group Acceptor), TRPM Cation Channels, Presenilins

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Presenilin mutations linked to familial Alzheimer's disease cause an imbalance in phosphatidylinositol 4,5-bisphosphate metabolism

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