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Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE222266 | GEO | 2024/03/04

REPOSITORIES: GEO

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Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (RNA-Seq)

Project description:Exploring the mechanism of transformation and propagation of acute myeloid leukemia is still the key to solving its refractory and relapse-prone problems. Phase separation refers to the process of specific aggregation of biological macromolecules through multivalent binding, and then leads to the functional sectorization in cell. Despite the fact that phase separation has been related to the dysregulation of various cellular processes, its role in the malignant transformation and development of AML is still less characterized. Nucleolus, as a multilayer condensate formed by phase separation, is an important place for the initiation of ribosome formation, and its function is directly related to protein translation. High-resolution imaging and fluorescence recovery after photo-bleaching experiments decode the positive regulatory relationship between the phase separation of FBL and the structure and function of nucleoli. Here, we used polysome profiling coupled with RNA-seq to depict transcriptome of AML cells with or without FBL knockdown.

2024-03-04 | GSE222264 | GEO

Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (rRNA 2'-O-me modification)

Project description:Exploring the mechanism of transformation and propagation of acute myeloid leukemia is still the key to solving its refractory and relapse-prone problems. Phase separation refers to the process of specific aggregation of biological macromolecules through multivalent binding, and then leads to the functional sectorization in cell. Despite the fact that phase separation has been related to the dysregulation of various cellular processes, its role in the malignant transformation and development of AML is still less characterized. Nucleolus, as a multilayer condensate formed by phase separation, is an important place for the initiation of ribosome formation, and its function is directly related to protein translation.High-resolution imaging and fluorescence recovery after photo-bleaching experiments decode the positive regulatory relationship between the phase separation of FBL and the structure and function of nucleoli. Here, we used RiboMeth-seq to examine rRNA 2’-O-me modification changes influenced by FBL knockdown in AML cells.

2024-03-04 | GSE222265 | GEO

Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis

Project description:Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis

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Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (RNA-Seq)

Project description:Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (RNA-Seq)

| PRJNA918713 | ENA

Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (rRNA 2'-O-me modification)

Project description:Phase separation-competent FBL shapes nucleolar function and translation in leukemogenesis (rRNA 2'-O-me modification)

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C9orf72 Poly(PR) Dipeptide Repeats Disturb Biomolecular Phase Separation and Disrupt Nucleolar Function.

Project description:Repeat expansion in the C9orf72 gene is the most common cause of the neurodegenerative disorder amyotrophic lateral sclerosis (C9-ALS) and is linked to the unconventional translation of five dipeptide-repeat polypeptides (DPRs). The two enriched in arginine, poly(GR) and poly(PR), infiltrate liquid-like nucleoli, co-localize with the nucleolar protein nucleophosmin (NPM1), and alter the phase separation behavior of NPM1 in vitro. Here, we show that poly(PR) DPRs bind tightly to a long acidic tract within the intrinsically disordered region of NPM1, altering its phase separation with nucleolar partners to the extreme of forming large, soluble complexes that cause droplet dissolution in vitro. In cells, poly(PR) DPRs disperse NPM1 from nucleoli and entrap rRNA in static condensates in a DPR-length-dependent manner. We propose that R-rich DPR toxicity involves disrupting the role of phase separation by NPM1 in organizing ribosomal proteins and RNAs within the nucleolus.

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LIN28 Promotes Nucleolar/Ribosomal Functions and Phase Separation in Pluripotent Stem Cells

Project description:This SuperSeries is composed of the SubSeries listed below.

2021-09-15 | GSE164420 | GEO

The role of phase separation in EBF1 pioneering function

Project description:This SuperSeries is composed of the SubSeries listed below.

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Aberrant phase separation and nucleolar dysfunction in rare genetic diseases.

Project description:Thousands of genetic variants in protein-coding genes have been linked to disease. However, the functional impact of most variants is unknown as they occur within intrinsically disordered protein regions that have poorly defined functions1-3. Intrinsically disordered regions can mediate phase separation and the formation of biomolecular condensates, such as the nucleolus4,5. This suggests that mutations in disordered proteins may alter condensate properties and function6-8. Here we show that a subset of disease-associated variants in disordered regions alter phase separation, cause mispartitioning into the nucleolus and disrupt nucleolar function. We discover de novo frameshift variants in HMGB1 that cause brachyphalangy, polydactyly and tibial aplasia syndrome, a rare complex malformation syndrome. The frameshifts replace the intrinsically disordered acidic tail of HMGB1 with an arginine-rich basic tail. The mutant tail alters HMGB1 phase separation, enhances its partitioning into the nucleolus and causes nucleolar dysfunction. We built a catalogue of more than 200,000 variants in disordered carboxy-terminal tails and identified more than 600 frameshifts that create arginine-rich basic tails in transcription factors and other proteins. For 12 out of the 13 disease-associated variants tested, the mutation enhanced partitioning into the nucleolus, and several variants altered rRNA biogenesis. These data identify the cause of a rare complex syndrome and suggest that a large number of genetic variants may dysregulate nucleoli and other biomolecular condensates in humans.

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Dynamic nucleolar phase separation influenced by non-canonical function of LIN28A instructs pluripotent stem cell fate decisions.

Project description:LIN28A is important in somatic reprogramming and pluripotency regulation. Although previous studies addressed that LIN28A can repress let-7 microRNA maturation in the cytoplasm, few focused on its role within the nucleus. Here, we show that the nucleolus-localized LIN28A protein undergoes liquid-liquid phase separation (LLPS) in mouse embryonic stem cells (mESCs) and in vitro. The RNA binding domains (RBD) and intrinsically disordered regions (IDR) of LIN28A contribute to LIN28A and the other nucleolar proteins' phase-separated condensate establishment. S120A, S200A and R192G mutations in the IDR result in subcellular mislocalization of LIN28A and abnormal nucleolar phase separation. Moreover, we find that the naive-to-primed pluripotency state conversion and the reprogramming are associated with dynamic nucleolar remodeling, which depends on LIN28A's phase separation capacity, because the LIN28A IDR point mutations abolish its role in regulating nucleolus and in these cell fate decision processes, and an exogenous IDR rescues it. These findings shed light on the nucleolar function in pluripotent stem cell states and on a non-canonical RNA-independent role of LIN28A in phase separation and cell fate decisions.

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