TRAMM/TrappC12 plays a role in chromosome congression, kinetochore stability, and CENP-E recruitment

Chromosome congression requires the stable attachment of microtubules to chromosomes mediated by the kinetochore, a large proteinaceous structure whose mechanism of assembly is unknown. In this paper, we present the finding that a protein called TRAMM (formerly known as TrappC12) plays a role in mit...

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Published inThe Journal of cell biology Vol. 209; no. 2; pp. 221 - 234
Main Authors Milev, Miroslav P, Hasaj, Benedeta, Saint-Dic, Djenann, Snounou, Sary, Zhao, Qingchuan, Sacher, Michael
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 27.04.2015
The Rockefeller University Press
Subjects
Blotting, Western
Cell division
Chromosomal Proteins, Non-Histone - metabolism
Chromosome Positioning
Chromosome Segregation
Chromosomes
Chromosomes, Human
Correlation analysis
HeLa Cells
Humans
Kinetochores - chemistry
Kinetochores - metabolism
Microtubules - metabolism
Mitosis - physiology
Phosphorylation
Proteins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spindle Apparatus
Two-Hybrid System Techniques
Vesicular Transport Proteins - metabolism
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Summary:Chromosome congression requires the stable attachment of microtubules to chromosomes mediated by the kinetochore, a large proteinaceous structure whose mechanism of assembly is unknown. In this paper, we present the finding that a protein called TRAMM (formerly known as TrappC12) plays a role in mitosis. Depletion of TRAMM resulted in noncongressed chromosomes and arrested cells in mitosis. Small amounts of TRAMM associated with chromosomes, and its depletion affected the localization of some kinetochore proteins, the strongest effect being seen for CENP-E. TRAMM interacts with CENP-E, and depletion of TRAMM prevented the recruitment of CENP-E to the kinetochore. TRAMM is phosphorylated early in mitosis and dephosphorylated at the onset of anaphase. Interestingly, this phosphorylation/dephosphorylation cycle correlates with its association/disassociation with CENP-E. Finally, we demonstrate that a phosphomimetic form of TRAMM recruited CENP-E to kinetochores more efficiently than did the nonphosphorylatable mutant. Our study identifies a moonlighting function for TRAMM during mitosis and adds a new component that regulates kinetochore stability and CENP-E recruitment.
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ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201501090