Proteomics

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Acetylation Regulates MARK2 activity

ABSTRACT: This study investigates the interactions between two enzymes involved in regulating the protein tau’s PTMs: the kinase MARK2 and the acetyltransferase CBP. Western blot analysis revealed that CBP-mediated acetylation was increased in the absence of MARK2, indicating a possible negative feedback loop, where MARK2 is inhibiting CBP acetylation. In contrast, inactive MARK2 (MARK2-KR) was strongly acetylated in the presence of acetyl-CBP, consistent with the preferential CBP binding and targeting of the inactive MARK2 conformation. To determine the specific lysine residues in MARK2 that are subject to acetylation in the presence of CBP, we immunopurified MARK2-KR alone (as a control) and CBP-acetylated MARK2-KR. We analyzed the immunopurified MARK2-KR by mass spectrometry-based proteomics to determine differential acetyl and phosphorylation sites.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Laura Herring  

LAB HEAD: Todd Cohen

PROVIDER: PXD030937 | Pride | 2022-06-09

REPOSITORIES: Pride

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20190823_PC630-Cohen_S1_Rep1.raw Raw
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Publications

Identification of a reciprocal negative feedback loop between tau-modifying proteins MARK2 kinase and CBP acetyltransferase.

Tabassum Zarin Z   Tseng Jui-Heng JH   Isemann Camryn C   Tian Xu X   Chen Youjun Y   Herring Laura E LE   Cohen Todd J TJ  

The Journal of biological chemistry 20220422 6

The posttranslational regulation of the neuronal proteome is critical for brain homeostasis but becomes dysregulated in the aged or diseased brain, in which abnormal posttranslational modifications (PTMs) are frequently observed. While the full extent of modified substrates that comprise the "PTM-ome" are slowly emerging, how the upstream enzymes catalyzing these processes are regulated themselves is not well understood, particularly in the context of neurodegeneration. Here, we describe the rec  ...[more]

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