Mutations in Tau’s Proline Rich Domain Affect its Protein Interactions

Co-IP mass spectrometry of the R221A and AxxA6 mouse lines revealed that mutations in tau's proline rich domain to affect tau's interactions with multiple proteins. Of the significant proteins, multiple are related to microtubule, metabolic, synaptic, and mitochondrial activity, and many are found within prion disease pathways and VEGF signaling pathways. Interestingly, PLCγ1 and p85α/PI3K, are also implicated in VEGF signaling pathways. These findings highlight the importance of further investigating the possible relationships between noted cellular processes and biological pathways and tau-protein interactions in familial AD.

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Publication Details

Journal
Alzheimer s & Dementia
Published
2024-12-01
DOI
https://doi.org/10.1002/alz.089653
Primary Topic
Alzheimer's disease research and treatments
Type
article
Field-Weighted Citation Impact
0.00
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Mutations in Tau’s Proline Rich Domain Affect its Protein Interactions

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Mutations in Tau’s Proline Rich Domain Affect its Protein Interactions

Kwaku Addo‐Osafo, Whitaker Cohn, Brittany M. Katz, Keith Vossel, Kaylin Hwang, Anne Koutures
article en

Abstract

Co-IP mass spectrometry of the R221A and AxxA6 mouse lines revealed that mutations in tau's proline rich domain to affect tau's interactions with multiple proteins. Of the significant proteins, multiple are related to microtubule, metabolic, synaptic, and mitochondrial activity, and many are found within prion disease pathways and VEGF signaling pathways. Interestingly, PLCγ1 and p85α/PI3K, are also implicated in VEGF signaling pathways. These findings highlight the importance of further investigating the possible relationships between noted cellular processes and biological pathways and tau-protein interactions in familial AD.

Alzheimer s & DementiaVol. 20(S1)
University of California, Los Angeles (US), UCLA Health (US), Foundation for Psychocultural Research (US)
Openalex Percentile: Top 66%
Alzheimer's disease research and treatments
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