Added by | eric_julien |
---|---|
Group name | EquipeEJ |
Item Type | Journal Article |
Title | High-resolution live-cell imaging reveals novel cyclin A2 degradation foci involving autophagy |
Creator | Loukil et al. |
Author | Abdelhalim Loukil |
Author | Manuela Zonca |
Author | Cosette Rebouissou |
Author | Véronique Baldin |
Author | Olivier Coux |
Author | Martine Biard-Piechaczyk |
Author | Jean-Marie Blanchard |
Author | Marion Peter |
Abstract | Cyclin A2 is a key player in the regulation of the cell cycle. Its degradation in mid-mitosis relies on the ubiquitin-proteasome system (UPS). Using high-resolution microscopic imaging, we find that cyclin A2 persists beyond metaphase. Indeed, we identify a novel cyclin-A2-containing compartment that forms dynamic foci. Förster (or fluorescence) resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy (FLIM) analyses show that cyclin A2 ubiquitylation takes place predominantly in these foci before spreading throughout the cell. Moreover, inhibition of autophagy in proliferating cells induces the stabilisation of a subset of cyclin A2, whereas induction of autophagy accelerates the degradation of cyclin A2, thus showing that autophagy is a novel regulator of cyclin A2 degradation. |
Publication | Journal of Cell Science |
Volume | 127 |
Issue | Pt 10 |
Pages | 2145-2150 |
Date | May 15, 2014 |
Journal Abbr | J. Cell. Sci. |
Language | eng |
DOI | 10.1242/jcs.139188 |
ISSN | 1477-9137 |
Library Catalog | PubMed |
Extra | PMID: 24634511 |
Tags | Autophagy, Cell Communication, Cyclin A2, FLIM, Fluorescence Resonance Energy Transfer, FRET, Humans, MCF-7 Cells, Microscopy, Fluorescence, original, Proteasome Endopeptidase Complex, Ubiquitin, Ubiquitin-proteasome system |
Date Added | 2019/05/28 - 13:52:53 |
Date Modified | 2019/05/28 - 13:58:44 |
Notes and Attachments | PubMed entry (Attachment) Texte intégral (Attachment) |