Proteomics

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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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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 spindle<sup>1</sup>. The reformation of sealed nuclei requires ESCRTs (endosomal sorting complexes required for transport) and LEM2, a transmembrane ESCRT adaptor<sup>2-4</sup>. 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 chromatin<sup>5  ...[more]

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