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DDA3 associates with microtubule plus ends and orchestrates microtubule dynamics and directional cell migration.


ABSTRACT: Cell motility and adhesion involve orchestrated interaction of microtubules (MTs) with their plus-end tracking proteins (+TIPs). However, the mechanisms underlying regulations of MT dynamics and directional cell migration are still elusive. Here, we show that DDA3-EB1 interaction orchestrates MT plus-end dynamics and facilitates directional cell migration. Biochemical characterizations reveal that DDA3 interacts with EB1 via its SxIP motif within the C-terminal Pro/Ser-rich region. Time-lapse and total internal reflection fluorescence (TIRF) microscopic assays demonstrate that DDA3 exhibits EB1-dependent, MT plus-end loading and tracking. The EB1-based loading of DDA3 is responsible for MT plus-ends stabilization at the cell cortex, which in turn orchestrates directional cell migration. Interestingly, the DDA3-EB1 interaction is potentially regulated by EB1 acetylation, which may account for physiological regulation underlying EGF-elicited cell migration. Thus, the EB1-based function of DDA3 links MT dynamics to directional cell migration.

SUBMITTER: Zhang L 

PROVIDER: S-EPMC3647168 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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DDA3 associates with microtubule plus ends and orchestrates microtubule dynamics and directional cell migration.

Zhang Liangyu L   Shao Hengyi H   Zhu Tongge T   Xia Peng P   Wang Zhikai Z   Liu Lifang L   Yan Maomao M   Hill Donald L DL   Fang Guowei G   Chen Zhengjun Z   Wang Dongmei D   Yao Xuebiao X  

Scientific reports 20130101


Cell motility and adhesion involve orchestrated interaction of microtubules (MTs) with their plus-end tracking proteins (+TIPs). However, the mechanisms underlying regulations of MT dynamics and directional cell migration are still elusive. Here, we show that DDA3-EB1 interaction orchestrates MT plus-end dynamics and facilitates directional cell migration. Biochemical characterizations reveal that DDA3 interacts with EB1 via its SxIP motif within the C-terminal Pro/Ser-rich region. Time-lapse an  ...[more]

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