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Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression

ABSTRACT: Cancer invasion and metastasis are governed by intricate molecular mechanisms. We demonstrate that TRIM27, an E3 ubiquitin ligase, plays dichotomous roles in cancer depending on its subcellular localization, which is controlled by acetylation/deacetylation at K297 independent of its ligase activity. Acetylation by GCN5 directs TRIM27 to the nucleus, while deacetylation by HDAC4 promotes cytoplasmic localization and cell proliferation. Nuclear TRIM27 binds PARP1 and NELFs, represses PARP1-mediated NELFA ADP-ribosylation, maintains RNA polymerase II pausing, and suppresses PAX6 transcription, thereby inhibiting cancer invasion and metastasis.

ORGANISM(S): Homo sapiens

PROVIDER: GSE327188 | GEO | 2026/04/27

REPOSITORIES: GEO

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Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression [CUT&Tag]

Project description:Cancer invasion and metastasis are orchestrated by intricate molecular mechanisms that remain not fully understood. We have identified that the tripartite motif-containing protein 27 (TRIM27), typically known as an E3 ubiquitin ligase, plays dichotomous roles in cancer progression. These roles are determined by its subcellular localization, which is regulated by acetylation and deacetylation at lysine 297 (K297) independently of its ubiquitin ligase activity. Acetylation by general control non-repressed protein 5 (GCN5) directs TRIM27 to the nucleus, where it inhibits cancer cell invasion and metastasis by modulating the transcription of paired box 6 (PAX6). Conversely, deacetylation by histone deacetylase 4 (HDAC4) results in cytoplasmic localization, promoting cell proliferation and tumor growth. In the nucleus, TRIM27 binds to poly (ADP-ribose) polymerase 1 (PARP1) and negative elongation factors (NELFs), repressing PARP1-mediated mono-ADP-ribosylation of NELFA, thereby preventing the release of RNA polymerase II from transcriptional pausing, and leading to transcriptional repression of PAX6. Furthermore, we demonstrate that treatment with the PARP1 inhibitor Olaparib limits the metastasis of cancer cells lacking breast cancer gene (BRCA) mutations, uncovering a previously overlooked therapeutic potential. Importantly, the combination of Olaparib and the HDAC4 inhibitor Tasquinimod synergistically inhibits cancer metastasis. Collectively, these findings reveal a complex interplay of post-translational modifications that dictate the subcellular localization and biological functions of TRIM27, highlighting novel strategies for effective cancer treatment.

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Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression [CUT&Tag II]

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Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression [CUT&Tag]

Project description:Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression [CUT&Tag]

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Dynamic acetylation/deacetylation dictates TRIM27 nuclear-cytoplasmic localization for cancer progression [CUT&Tag II]

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Temporal regulation of PARP1 acetylation in tumorigenesis

Project description:We examined the impact of PARP1-ATF4 interaction on cellular transcription program. ATF4 plays a pivotal role in stress response by regulating expression of diverse genes. Under genotoxic stress, the acetylation status of PARP1 at lysine 521 influences the expression of diverse genes. Also, co-depletion of ATF4 leads to the downregulation of many genes. These genes are involved in pathways related to cancer risk, such as epithelial-to-mesenchymal transition (EMT), metastasis, cell cycle regulation, and metabolic processes.

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