Publication Date:
2005-12-03
Description:
Proper chromosome segregation requires the attachment of sister kinetochores to microtubules from opposite spindle poles to form bi-oriented chromosomes on the metaphase spindle. The chromosome passenger complex containing Survivin and the kinase Aurora B regulates this process from the centromeres. We report that a de-ubiquitinating enzyme, hFAM, regulates chromosome alignment and segregation by controlling both the dynamic association of Survivin with centromeres and the proper targeting of Survivin and Aurora B to centromeres. Survivin is ubiquitinated in mitosis through both Lys(48) and Lys(63) ubiquitin linkages. Lys(63) de-ubiquitination mediated by hFAM is required for the dissociation of Survivin from centromeres, whereas Lys(63) ubiquitination mediated by the ubiquitin binding protein Ufd1 is required for the association of Survivin with centromeres. Thus, ubiquitinaton regulates dynamic protein-protein interactions and chromosome segregation independently of protein degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vong, Queenie P -- Cao, Kan -- Li, Hoi Y -- Iglesias, Pablo A -- Zheng, Yixian -- GM56312/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1499-504.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington and Howard Hughes Medical Institute, 3520 San Martin Drive, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322459" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Aurora Kinase B
;
Aurora Kinases
;
Centromere/*metabolism
;
Chromosomal Proteins, Non-Histone/metabolism
;
Chromosome Segregation/*physiology
;
Egg Proteins/metabolism
;
Endopeptidases/metabolism
;
HeLa Cells
;
Humans
;
Inhibitor of Apoptosis Proteins
;
Lysine/metabolism
;
Microtubule-Associated Proteins/metabolism
;
Molecular Sequence Data
;
Neoplasm Proteins/metabolism
;
Protein Binding
;
Protein-Serine-Threonine Kinases/metabolism
;
Ubiquitin/*metabolism
;
Ubiquitin Thiolesterase
;
Xenopus
;
Xenopus Proteins/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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