SCFSlimb ubiquitin ligase suppresses condensin II–mediated nuclear reorganization by degrading Cap-H2

• DOI: 10.1083/jcb.201207183
• Publication Date: 2013-03-26T01:29:32Z
• Authors: Daniel W. Buster; Scott G. Daniel; Huy Q. Nguyen; Sarah L. Windler; Lara C. Skwarek; Maureen Peterson; Meredith Roberts; Joy H. Meserve; Tom Hartl; Joseph E. Klebba; David Bilder; Giovanni Bosco; Gregory C. Rogers
• Keywords: Condensin; Premature chromosome condensation; Interphase

Condensin complexes play vital roles in chromosome condensation during mitosis and meiosis. II uniquely localizes to chromatin throughout the cell cycle and, addition its mitotic duties, modulates organization gene expression interphase. Mitotic condensin activity is regulated by phosphorylation, but mechanisms that regulate interphase are unclear. Here, we report inactivated when subunit Cap-H2 targeted for degradation SCFSlimb ubiquitin ligase complex disruption of this process dramatically changed organization. Inhibition function reorganized chromosomes into dense, compact domains disrupted homologue pairing both cultured Drosophila cells vivo, these effects were rescued inactivation. Furthermore, stabilization distorted nuclear envelopes dispersed Cid/CENP-A on chromosomes. Therefore, SCFSlimb-mediated down-regulation required maintain proper morphology nucleus.