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Quantitative phosphoproteomics uncovers dysregulated kinase networks in Alzheimer’s disease

ABSTRACT: Alzheimer’s disease (AD) is a form of dementia characterized by amyloid-β plaques and Tau neurofibrillary tangles that progressively disrupt neural circuits in the brain. Using mass spectrometry, we performed a combined analysis of the tyrosine, serine, and threonine phosphoproteome, and proteome of post-mortem brain tissue from AD patients and aged matched controls. We used a data-centric approach to identify co-correlated signaling networks associated with cellular and pathological changes. We identified two independent pathology clusters that were associated with Tau and oligodendrocyte pathologies. We observed phosphorylation sites on known Tau-kinases as well as other novel signaling factors that were associated with these clusters. Together, these results build a map of pathology-associated phosphorylation signaling activation events occurring in AD.

INSTRUMENT(S): LTQ Orbitrap, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Nader Morshed

LAB HEAD: Forest Michael White

PROVIDER: PXD020087 | Pride | 2021-05-25

REPOSITORIES: Pride

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			Action	DRS
	2017-10-13-HAD1-pY-imac64-pre121-col125.raw	Raw
	2017-10-13-HAD1-pY-sup10-pre122-col114.RAW	Raw
	2017-10-19-HAD1-pST-col125-1.raw	Raw
	2017-10-19-HAD1-pST-col125-10.raw	Raw
	2017-10-19-HAD1-pST-col125-11.raw	Raw

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