PIP2 epigenetically represses rRNA genes transcription interacting with PHF8

Ulicna, Livia; Kalendová, Alžběta; Kalasová, Ilona; Vacı́k, Tomáš; Hozák, Pavel

doi:10.1016/j.bbalip.2017.12.008

Cited by 30 publications

(27 citation statements)

References 40 publications

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“…The majority of the PtdIns(3,4,5)P3-interactors identified in this study are characterised by the presence of at least one polybasic motif shown previously to serve as PPIn interaction sites via electrostatic interactions in other nuclear proteins (25,41,43,45,(48)(49)(50)(51)(52) or of basic patches, as found in nucleophosmin, ALY and OGT (42,44,64). This finding is consistent with the enrichment of such motifs in the nuclear PtdIns(4,5)P2 interactome that we have previously reported (46).…”

Section: Discussionmentioning

confidence: 65%

“…Several studies have identified multiple nuclear processes attributed to nuclear PPIn, including mRNA processing, splicing and export, chromatin remodelling, transcription as well as cell cycle progression (32)(33)(34)(35)(36)(37)(38). Nuclear PPIn regulate these processes by interacting electrostatically with proteins via plekstrin homology (PH) domain in few cases (39,40) but mostly via polybasic regions (PBR), also called K/R rich motifs ( (25,(41)(42)(43)(44)(45)(46)(47)(48)(49)(50)(51)(52), and recently reviewed in (7)). So far, PtdIns(4,5)P2, its metabolising enzymes and effector proteins have been identified in nuclear speckles, hubs of mRNA processing and export (20,21,44,53,54).…”

Section: Introductionmentioning

confidence: 99%

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Nuclear phosphatidylinositol 3,4,5-trisphosphate interactome uncovers an enrichment in nucleolar proteins

Gavgani

Morovicz

D’Santos

et al. 2020

Preprint

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Polyphosphoinositides (PPIn) play essential functions as lipid signalling molecules and many of their functions have been elucidated in the cytoplasm. However, PPIn are also intranuclear where they contribute to chromatin remodelling, transcription and mRNA splicing. The PPIn, phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) has been mapped to the nucleus and nucleoli but its role remains unclear in this subcellular compartment. To gain further insights into the nuclear functions of PtdIns(3,4,5)P3, we applied a previously developed quantitative mass spectrometry-based approach to identify the targets of PtdIns(3,4,5)P3 from isolated nuclei. We identified 179 potential PtdIns(3,4,5)P3-interacting proteins and gene ontology analysis for the biological functions of this dataset revealed an enrichment in RNA processing/splicing, cytokinesis, protein folding and DNA repair. Interestingly, about half of these interactors were common to nucleolar protein datasets, some of which had dual functions in rRNA transcription and DNA repair, including Poly(ADP-Ribose) Polymerase 1 (PARP1/ARTD1). PARP1 was found to interact directly with PtdIns(3,4,5)P3 as well as PtdIns(3,4)P2 and to co-localise with PtdIns(3,4,5)P3 in the nucleolus and with PtdIns(3,4)P2 in nucleoplasmic foci. In conclusion, the PtdIns(3,4,5)P3 interactome reported here identified several nucleolar proteins and further pointed to roles for this lipid in these processes.

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Section: Discussionmentioning

confidence: 65%

Section: Introductionmentioning

confidence: 99%

Nuclear phosphatidylinositol 3,4,5-trisphosphate interactome uncovers an enrichment in nucleolar proteins

Gavgani

Morovicz

D’Santos

et al. 2020

Preprint

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“…Nascent RNA and proteins involved in Pol II transcription colocalise with nucleoplasmic PtdIns(4,5)P 2 islets Previously published data have shown that PtdIns(4,5)P 2 is pulled down by Pol II (Osborne et al, 2001) and binds to Pol I transcription machinery (Sobol et al, 2013;Ulicna et al, 2018;Yildirim et al, 2013). These findings prompted us to study the particular transcription-related proteins associated with nucleoplasmic PtdIns(4,5)P 2 .…”

Section: Resultsmentioning

confidence: 95%

Nuclear phosphatidylinositol 4,5-bisphosphate islets contribute to efficient RNA polymerase II-dependent transcription

Sobol

Krausová

Yıldırım

et al. 2018

Journal of Cell Science

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This paper describes a novel type of nuclear structure - nuclear lipid islets (NLIs). They are of 40-100 nm with a lipidic interior, and phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P] molecules comprise a significant part of their surface. Most of NLIs have RNA at the periphery. Consistent with that, RNA is required for their integrity. The NLI periphery is associated with Pol II transcription machinery, including the largest Pol II subunit, transcription factors and NM1 (also known as NMI). The PtdIns(4,5)P-NM1 interaction is important for Pol II transcription, since NM1 knockdown reduces the Pol II transcription level, and the overexpression of wild-type NM1 [but not NM1 mutated in the PtdIns(4,5)P-binding site] rescues the transcription. Importantly, Pol II transcription is dependent on NLI integrity, because an enzymatic reduction of the PtdIns(4,5)P level results in a decrease of the Pol II transcription level. Furthermore, about half of nascent transcripts localise to NLIs, and transcriptionally active transgene loci preferentially colocalise with NLIs. We hypothesize that NLIs serve as a structural platform that facilitates the formation of Pol II transcription factories, thus participating in the formation of nuclear architecture competent for transcription.

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“…PIs form just a minor fraction of the total phospholipid content in eukaryotic cell membranes. However, they function in diverse roles, ranging from regulating essential biological processes such as cell adhesion [7], migration [8], apoptosis [9], vesicular trafficking [10], to post-translational modifications [11]. All these cellular processes are consistent with the hallmarks of cancer.…”

Section: Introductionmentioning

confidence: 99%

Phosphoinositide-Dependent Signaling in Cancer: A Focus on Phospholipase C Isozymes

Obeng

Rusciano

Marvi

et al. 2020

IJMS

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Phosphoinositides (PI) form just a minor portion of the total phospholipid content in cells but are significantly involved in cancer development and progression. In several cancer types, phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] and phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] play significant roles in regulating survival, proliferation, invasion, and growth of cancer cells. Phosphoinositide-specific phospholipase C (PLC) catalyze the generation of the essential second messengers diacylglycerol (DAG) and inositol 1,4,5 trisphosphate (InsP3) by hydrolyzing PtdIns(4,5)P2. DAG and InsP3 regulate Protein Kinase C (PKC) activation and the release of calcium ions (Ca2+) into the cytosol, respectively. This event leads to the control of several important biological processes implicated in cancer. PLCs have been extensively studied in cancer but their regulatory roles in the oncogenic process are not fully understood. This review aims to provide up-to-date knowledge on the involvement of PLCs in cancer. We focus specifically on PLCβ, PLCγ, PLCδ, and PLCε isoforms due to the numerous evidence of their involvement in various cancer types.

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PIP2 epigenetically represses rRNA genes transcription interacting with PHF8

Cited by 30 publications

References 40 publications

Nuclear phosphatidylinositol 3,4,5-trisphosphate interactome uncovers an enrichment in nucleolar proteins

Nuclear phosphatidylinositol 3,4,5-trisphosphate interactome uncovers an enrichment in nucleolar proteins

Nuclear phosphatidylinositol 4,5-bisphosphate islets contribute to efficient RNA polymerase II-dependent transcription

Phosphoinositide-Dependent Signaling in Cancer: A Focus on Phospholipase C Isozymes

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