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Two NEMO-like Ubiquitin-Binding Domains in CEP55 Differently Regulate Cytokinesis.

iScience (2019-10-13)
Keïs Nabhane Said Halidi, Elisabeth Fontan, Alix Boucharlat, Laurianne Davignon, Marine Charpentier, Mikaël Boullé, Robert Weil, Alain Israël, Emmanuel Laplantine, Fabrice Agou
ABSTRACT

CEP55 regulates the final critical step of cell division termed cytokinetic abscission. We report herein that CEP55 contains two NEMO-like ubiquitin-binding domains (UBDs), NOA and ZF, which regulate its function in a different manner. In vitro studies of isolated domains showed that NOA adopts a dimeric coiled-coil structure, whereas ZF is based on a UBZ scaffold. Strikingly, CEP55 knocked-down HeLa cells reconstituted with the full-length CEP55 ubiquitin-binding defective mutants, containing structure-guided mutations either in NOACEP55 or ZFCEP55 domains, display severe abscission defects. In addition, the ZFCEP55 can be functionally replaced by some ZF-based UBDs belonging to the UBZ family, indicating that the essential function of ZFCEP55 is to act as ubiquitin receptor. Our work reveals an unexpected role of CEP55 in non-degradative ubiquitin signaling during cytokinetic abscission and provides a molecular basis as to how CEP55 mutations can lead to neurological disorders such as the MARCH syndrome.

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Monoclonal Anti-β-Tubulin antibody produced in mouse, clone TUB 2.1, ascites fluid