Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1932482 | Biochemical and Biophysical Research Communications | 2010 | 5 Pages |
Abstract
DDA3 is a microtubule-associated protein that controls chromosome congression and segregation by regulating the mitotic spindle. Depletion of DDA3 alters spindle structure, generates unaligned chromosomes at metaphase, and delays the mitotic progression. Through a mass spectrometry analysis, we found that DDA3 is phosphorylated on Ser225 during mitosis. Phosphorylation of this residue is important for the mitotic function of DDA3, as the phospho-mimicking DDA3-S225D variant, but not the nonphosphorable DDA3-S225A mutant, rescues the DDA3-knockdown phenotype. We conclude that the mitotic function of DDA3 is regulated by phosphorylation on the Ser225 residue.
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Authors
Chang-Young Jang, Judith A. Coppinger, John R. Yates III, Guowei Fang,