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Cell-type-specific TEV protease cleavage reveals cohesin functions in Drosophila neurons

Title data

Pauli, Andrea ; Althoff, Friederike ; Oliveira, Raquel A. ; Heidmann, Stefan ; Schuldiner, Oren ; Lehner, Christian F. ; Dickson, Barry J. ; Nasmyth, Kim:
Cell-type-specific TEV protease cleavage reveals cohesin functions in Drosophila neurons.
In: Developmental Cell. Vol. 14 (2008) Issue 2 . - pp. 239-251.
ISSN 1878-1551
DOI: https://doi.org/10.1016/j.devcel.2007.12.009

Abstract in another language

Cohesin is a highly conserved multisubunit complex that holds sister chromatids together in mitotic cells. At the metaphase to anaphase transition, proteolytic cleavage of the alpha kleisin subunit (Rad21) by separase causes cohesin's dissociation from chromosomes and triggers sister-chromatid disjunction. To investigate cohesin's function in postmitotic cells, where it is widely expressed, we have created fruit flies whose Rad21 can be cleaved by TEV protease. Cleavage causes precocious separation of sister chromatids and massive chromosome missegregation in proliferating cells, but not disaggregation of polytene chromosomes in salivary glands. Crucially, cleavage in postmitotic neurons is lethal. In mushroom-body neurons, it causes defects in axon pruning, whereas in cholinergic neurons it causes highly abnormal larval locomotion. These data demonstrate essential roles for cohesin in nondividing cells and also introduce a powerful tool by which to investigate protein function in metazoa.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Sister-Chromatid Cohesion; De-Lange-Syndrome; Gene-Expression; Axonal Migrations; Turning Behavior; SMC Proteins; Nipped-B; CHromosome; Homolog; Localization
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Result of work at the UBT: No
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 05 Mar 2020 10:08
Last Modified: 26 Oct 2022 12:35
URI: https://eref.uni-bayreuth.de/id/eprint/54470