Human Nudel and NudE as Regulators of Cytoplasmic Dynein in Poleward Protein Transport along the Mitotic Spindle

• DOI: 10.1128/mcb.23.4.1239-1250.2003
• Publication Date: 2003-01-29T22:44:28Z
• Authors: Xiumin Yan; Fang Li; Yun Liang; Yidong Shen; Xiangshan Zhao; Qiongping Huang; Xueliang Zhu
• Keywords: Dynactin; Spindle pole body; Transport protein; Microtubule organizing center

Emerging evidence supports the idea that a signaling pathway containing orthologs of at least mammalian NudE and Nudel, Lis1, cytoplasmic dynein is conserved for eukaryotic nuclear migration. In mammals, this has profound impact on neuronal migration during development central nervous system. Lis1 are also involved in other cellular functions, such as mitosis. Here we show Nudel participates subset function M phase. was specifically phosphorylated phase its serine/threonine phosphorylation motifs, probably by Cdc2 Erk1 -2. A fraction bound to centrosomes strongly interphase localized mitotic spindles early By using mutants incapable or simulating phosphorylation, confirmed regulated cell-cycle-dependent distribution, possibly increasing dissociation rate microtubule-organizing center. Moreover, phosphorylation-mimicking mutant more efficiently. We further demonstrated binding impaired poleward movement hence dynein-mediated transport kinetochore proteins spindle poles along microtubules, process contributing inactivation checkpoint These results point importance Nudel-Lis1 interaction activity possible role facilitating interaction. addition, comparative studies suggest functionally related paralog, Nudel.