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Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

ABSTRACT: Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

PROVIDER: PRJNA657068 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12450600_1.fastq.gz	Fastqsanger.gz
	SRR12450600_2.fastq.gz	Fastqsanger.gz
	SRR12450581_1.fastq.gz	Fastqsanger.gz
	SRR12450581_2.fastq.gz	Fastqsanger.gz
	SRR12450582_1.fastq.gz	Fastqsanger.gz

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Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

Project description:Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

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Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [RNA-seq]

Project description:Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [RNA-seq]

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Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [ChIP-seq]

Project description:Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [ChIP-seq]

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Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

Project description:Processing bodies (PBs) and stress granules (SGs) are prominent examples of subcellular, membrane-less compartments that are observed under physiological and stress conditions, respectively. We observe that the trimeric PB protein DCP1A rapidly (within ~10 s) phase-separates in mammalian cells during hyperosmotic stress and dissolves upon isosmotic rescue (over ~100 s) with minimal impact on cell viability even after multiple cycles of osmotic perturbation. Strikingly, this rapid intracellular hyperosmotic phase separation (HOPS) correlates with the degree of cell volume compression, distinct from SG assembly, and is exhibited broadly by homo-multimeric (valency ≥ 2) proteins across several cell types. Notably, HOPS sequesters pre-mRNA cleavage factor components from actively transcribing genomic loci, providing a mechanism for hyperosmolarity-induced global impairment of transcription termination. Together, our data suggest that the multimeric proteome rapidly responds to changes in hydration and molecular crowding, revealing an unexpected mode of globally programmed phase separation and sequestration that adapts the cell to volume change.

2020-09-17 | GSE154123 | GEO

Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [ChIP-seq]

2020-08-14 | GSE156227 | GEO

Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change [RNA-seq]

2020-08-14 | GSE156226 | GEO

Multivalent proteins rapidly and reversibly phase-separate upon osmotic cell volume change

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

2020-08-14 | GSE156228 | GEO

Multivalent Proteins Rapidly and Reversibly Phase-Separate upon Osmotic Cell Volume Change.

Project description:Processing bodies (PBs) and stress granules (SGs) are prominent examples of subcellular, membraneless compartments that are observed under physiological and stress conditions, respectively. We observe that the trimeric PB protein DCP1A rapidly (within ∼10 s) phase-separates in mammalian cells during hyperosmotic stress and dissolves upon isosmotic rescue (over ∼100 s) with minimal effect on cell viability even after multiple cycles of osmotic perturbation. Strikingly, this rapid intracellular hyperosmotic phase separation (HOPS) correlates with the degree of cell volume compression, distinct from SG assembly, and is exhibited broadly by homo-multimeric (valency ≥ 2) proteins across several cell types. Notably, HOPS sequesters pre-mRNA cleavage factor components from actively transcribing genomic loci, providing a mechanism for hyperosmolarity-induced global impairment of transcription termination. Our data suggest that the multimeric proteome rapidly responds to changes in hydration and molecular crowding, revealing an unexpected mode of globally programmed phase separation and sequestration.

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Cell volume controlled by LRRC8A-formed volume-regulated anion channels fine-tunes T cell activation and function

Project description:To become fully functional effector T cells, naïve T cells undergo a drastic metabolic status shift from quiescence to substantial biosynthesis. The synthesis of biomass initiated by T cell receptor (TCR) signals drives the cell volume increase during T cell activation (T lymphoblast), which resembles the slowest extreme of hypotonic cell swelling. However, the fundamental role of cell volume regulation in TCR signaling during T lymphoblast and its underlying mechanisms remain a long-standing enigma. Here we show that optimal T cell activation and function require appropriate cell volume regulation by regulated volume decrease (RVD) mediated via volume-regulated anion channels (VRACs) during T cell blast. Pharmacological blockade of VRACs and genetic deletion of LRRC8A in T cells, the essential component of VRACs, impair T cell activation and function, particularly under weak TCR stimulation, such as low-affinity TCR-pMHC engagement and unsaturated anti-CD3e crosslinking. Additionally, LRRC8A has distinct influences on mRNA transcriptional profiles driven by various TCR signal strengths, revealing the prominent effects of cell volume regulation for T cell functions. More importantly, LRRC8A-deficient mice have defective antiviral immunity and obstacles in effector-memory transition of CD8+ T cells. Furthermore, LRRC8A escorts the thymic selection of T cells and shapes the T cell repertoire in the thymus. Mechanistically, LRRC8A governs stringent cell volume increase via RVD during T cell blast induced by activation-driven intracellular osmolytes accumulation to keep the proximal TCR signaling molecules at adequate density. T cell blast driven by TCR signal feedbacks to control T cell activation. Together, our results reveal a previously unappreciated layer of T cell activation regulation that LRRC8A acts as a cell volume controlling "valve" to facilitate T cell activation and function

2023-09-23 | GSE243574 | GEO

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