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XB-ART-42018
Cell August 6, 2010; 142 (3): 444-55.

Aurora kinases and protein phosphatase 1 mediate chromosome congression through regulation of CENP-E.

Kim Y , Holland AJ , Lan W , Cleveland DW .


Abstract
Opposing roles of Aurora kinases and protein phosphatase 1 (PP1) during mitosis have long been suggested. Here, we demonstrate that Aurora kinases A and B phosphorylate a conserved residue on the kinetochore motor CENP-E. PP1 binds CENP-E via a motif overlapping this phosphorylation site and binding is disrupted by Aurora phosphorylation. Phosphorylation of CENP-E by the Auroras is enriched at spindle poles, disrupting binding of PP1 and reducing CENP-E''s affinity for individual microtubules. This phosphorylation is required for CENP-E-mediated towing of initially polar chromosomes toward the cell center. Kinetochores on such chromosomes cannot make subsequent stable attachment to spindle microtubules when dephosphorylation of CENP-E or rebinding of PP1 to CENP-E is blocked. Thus, an Aurora/PP1 phosphorylation switch modulates CENP-E motor activity as an essential feature of chromosome congression from poles and localized PP1 delivery by CENP-E to the outer kinetochore is necessary for stable microtubule capture by those chromosomes.

PubMed ID: 20691903
PMC ID: PMC2921712
Article link: Cell
Grant support: [+]
Genes referenced: aurka aurkb cenpe dld h2bc21 incenp myc npy4r ptk2 tacc3 tbx2


Article Images: [+] show captions
References [+] :
Akiyoshi, Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit. 2009, Pubmed


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