Borealin interacts directly with Snf7/Shrb/CHMP4 components in both Drosophila and human cells and the two proteins colocalize at the midbody in late cytokinesis.
| Inventor | Institute |
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| P Paolo D'Avino | University of Cambridge |
| SKU: | 151827 |
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| Product description: | Borealin interacts directly with Snf7/Shrb/CHMP4 components in both Drosophila and human cells and the two proteins colocalize at the midbody in late cytokinesis. Aurora B phosphorylates CHMP4C at three serine residues located in its C-terminal linker region, a part of the protein known to regulate its ability to form polymers and interact with the membrane. Over-expression of CHMP4C variants mutated in these three residues caused cytokinesis failure, suggesting that Aurora B inhibits CHMP4C activity during cytokinesis. It is proposed that CPC controls abscission timing in both flies and human cells by regulating the function of ESCRT-III Snf7 proteins during cytokinesis through the interaction of its Borealin component with the N-terminus of Shrb/CHMP4 proteins and Aurora B-mediated phosphorylation of the CHMP4C regulatory linker tail. |
| Conjugation: | Unconjugated |
| Molecular weight: | ~30 |
| Immunogen: | Synthetic peptide (TARRSRAASSQRAEEC) |
| Cat. #: | 151827 |
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| Provenance and Ownership: | The Anti-Phospho CHMP4C [pCHMP4C] is owned by Cancer Research UK. CancerTools supplies the Anti-Phospho CHMP4C [pCHMP4C] under licence from Cancer Research UK and is the authorised source for its distribution. Sourcing Anti-Phospho CHMP4C [pCHMP4C] directly from the IP owner ensures authenticity, provenance and compliance with all applicable licensing and research use requirements. |
| Unit size: | 100 ug |
| Research Fields: | Cell biology |
| Application: | WB |
| Target: | Phospho charged multi vesicular protein 4c |
| Reactivity: | Mammalian |
| Clone: | pCHMP4C |
| Host: | Rabbit |
| Class: | Polyclonal |
| Primary citation: | Capalbo et al. 2012. Open Biol. 2:120070 PMID: 22724069 |
| Target background: | Borealin interacts directly with Snf7/Shrb/CHMP4 components in both Drosophila and human cells and the two proteins colocalize at the midbody in late cytokinesis. Aurora B phosphorylates CHMP4C at three serine residues located in its C-terminal linker region, a part of the protein known to regulate its ability to form polymers and interact with the membrane. Over-expression of CHMP4C variants mutated in these three residues caused cytokinesis failure, suggesting that Aurora B inhibits CHMP4C activity during cytokinesis. It is proposed that CPC controls abscission timing in both flies and human cells by regulating the function of ESCRT-III Snf7 proteins during cytokinesis through the interaction of its Borealin component with the N-terminus of Shrb/CHMP4 proteins and Aurora B-mediated phosphorylation of the CHMP4C regulatory linker tail. |
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| Format: | Liquid |
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| Concentration: | 0.9-1.1mg/ml |
| Storage buffer: | PBS with 0.02% azide |
| Storage conditions: | -20° C |
| Shipping conditions: | Dry ice |
| References: |
Capalbo et al. 2012. Open Biol. 2:120070 PMID: 22724069 Petsalaki et al. 2016. Nat Commun. 7:11451. PMID: 27126587. |
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