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The Flemmingsome reveals an ESCRT-to-membrane coupling via ALIX/syntenin/syndecan-4 required for completion of cytokinesis
- Source :
- Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020), Nature Communications, Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.1941. ⟨10.1038/s41467-020-15205-z⟩, Nature Communications, 2020, 11 (1), pp.1941. ⟨10.1038/s41467-020-15205-z⟩
- Publication Year :
- 2020
- Publisher :
- Nature Portfolio, 2020.
-
Abstract
- Cytokinesis requires the constriction of ESCRT-III filaments on the side of the midbody, where abscission occurs. After ESCRT recruitment at the midbody, it is not known how the ESCRT-III machinery localizes to the abscission site. To reveal actors involved in abscission, we obtained the proteome of intact, post-abscission midbodies (Flemmingsome) and identified 489 proteins enriched in this organelle. Among these proteins, we further characterized a plasma membrane-to-ESCRT module composed of the transmembrane proteoglycan syndecan-4, ALIX and syntenin, a protein that bridges ESCRT-III/ALIX to syndecans. The three proteins are highly recruited first at the midbody then at the abscission site, and their depletion delays abscission. Mechanistically, direct interactions between ALIX, syntenin and syndecan-4 are essential for proper enrichment of the ESCRT-III machinery at the abscission site, but not at the midbody. We propose that the ESCRT-III machinery must be physically coupled to a membrane protein at the cytokinetic abscission site for efficient scission, uncovering common requirements in cytokinesis, exosome formation and HIV budding.<br />ESCRT filaments drive the final abscission between two daughter cells but how they physically interact with the membrane is unclear. Using proteomics, the authors show that syndecan-4/syntenin/ALIX couples the ESCRT machinery to the abscission site and thus promotes efficient abscission.
- Subjects :
- 0301 basic medicine
Syntenins
SYNDECAN
[SDV]Life Sciences [q-bio]
General Physics and Astronomy
Cell Cycle Proteins
Plasma protein binding
ABSCISSION
0302 clinical medicine
ALIX
SYNTENIN
lcsh:Science
Multidisciplinary
Chemistry
MOLECULAR-MECHANISMS
Transmembrane protein
3. Good health
Cell biology
[SDV] Life Sciences [q-bio]
Multidisciplinary Sciences
Midbody
Science & Technology - Other Topics
MACHINERY
LATE STEPS
Protein Binding
Cell division
Science
BIOGENESIS
SCISSION
HIV Budding
Endosomes
macromolecular substances
General Biochemistry, Genetics and Molecular Biology
ESCRT
Article
03 medical and health sciences
Abscission
Humans
Cytokinesis
Organelles
MIDBODY
Science & Technology
Endosomal Sorting Complexes Required for Transport
Calcium-Binding Proteins
Cell Membrane
General Chemistry
030104 developmental biology
Membrane protein
Syndecan-4
lcsh:Q
030217 neurology & neurosurgery
HeLa Cells
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 11
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....6078968e56a9ab111e62e49c7551a0a3