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

ABSTRACT: Identification of the specific acetylation sites on GST-TRIM27 modified by HA-GCN5 in vitro and the specific nuclear interaction partners of TRIM27 using mass spectrometry

ORGANISM(S): Homo Sapiens

SUBMITTER: Mian Wu

PROVIDER: PXD075537 | iProX | Wed Mar 11 00:00:00 GMT 2026

REPOSITORIES: iProX

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

Project description: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.

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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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