Dataset Information

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation

ABSTRACT: Quantitative crosslinking analysis to probe in vitro conformational dynamics governing ESCRT-mediated nuclear envelope formation. CHMP7 was crosslinked with D12-BS3 while CHMP7 in the presence of LEM2 winged helix domain was crosslinked with H12-BS3. Samples were mixed after crosslinking and analyzed according to standard procedures. The raw files included here correspond to four SEC fractions from a single experiment that contain crosslinked peptides.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Adam Frost

PROVIDER: MSV000084837 | MassIVE | Fri Jan 24 10:53:00 GMT 2020

REPOSITORIES: MassIVE

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Publications

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation.

von Appen Alexander A LaJoie Dollie D Johnson Isabel E IE Trnka Michael J MJ Pick Sarah M SM Burlingame Alma L AL Ullman Katharine S KS Frost Adam A

Nature 20200429 7810

During cell division, remodelling of the nuclear envelope enables chromosome segregation by the mitotic spindle1. The reformation of sealed nuclei requires ESCRTs (endosomal sorting complexes required for transport) and LEM2, a transmembrane ESCRT adaptor2-4. Here we show how the ability of LEM2 to condense on microtubules governs the activation of ESCRTs and coordinated spindle disassembly. The LEM motif of LEM2 binds BAF, conferring on LEM2 an affinity for chromatin5 ...[more]

PMID: 32494070

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Project description:Chloroplast is a major plant cell organelle that fulfills essential metabolic and biosynthetic functions. Located at the interface between the chloroplast and other cell compartments, the chloroplast envelope system is a strategic barrier controlling exchanges of ions, metabolites and proteins, thus regulating essential metabolic functions (synthesis of hormones precursors, amino acids, pigments, sugars, vitamins, lipids, nucleotides…) of the plant cell. However, chloroplast envelope membranes remain the hidden part of the chloroplast proteome and many envelope proteins remain to be characterized (known but uncharacterized envelope proteins) or identified (orphan known envelope-associated functions carried by unidentified proteins) Indeed, the envelope contains only 1% of the chloroplast proteins (i.e. 0.25% of the whole cell proteome). When comparing the composition crude leaf extract and purified envelope vesicles, a high theoretical enrichment factor (EF) of specific envelope proteins is thus expected. This is especially true for minor envelope proteins (e.g. representing 1/100 or 1/1000 of the envelope protein content). Sensitivity of MS technique has been greatly improved during the last decade. Today, thanks to the continuous improvement of MS techniques, we are able to detect more components in a complex sample, to generate quantitative data and to statistically validate above-cited enrichment factor. Here, we have taken advantage of present-days better MS sensitivity towards a better definition (differentiate genuine envelope proteins from contaminants) of the chloroplast envelope proteome. This MS- and statistical-based analysis relied on an enrichment factor calculated for each protein identified in purified envelope fractions when compared to the value obtained for the same protein in crude cell extracts. Using this approach, a total of 1376 proteins was detected in purified envelope fractions, of which, more than 500 could be assigned an envelope localization combining MS-based statistical analyses and manual annotation using data from the literature or prediction tools. Interestingly, many of such proteins being unknown or unexpected envelope components, these data constitute a new resource of significant value to the broader plant science community aiming to define principles and molecular mechanisms controlling fundamental aspects of plastid biogenesis and functions.

Dataset Information

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation

Publications

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation.

Similar Datasets

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