Oncotarget

Research Papers:

Phosphorylation of EB1 regulates the recruitment of CLIP-170 and p150glued to the plus ends of astral microtubules

Jie Ran, Youguang Luo, Yijun Zhang, Yang Yang, Miao Chen, Min Liu, Dengwen Li and Jun Zhou _

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Oncotarget. 2017; 8:9858-9867. https://doi.org/10.18632/oncotarget.14222

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Abstract

Jie Ran1,*, Youguang Luo2,*, Yijun Zhang2,*, Yang Yang2, Miao Chen1, Min Liu1, Dengwen Li2, Jun Zhou1,2

1Institute of Biomedical Sciences, College of Life Sciences, Key Laboratory of Animal Resistance Biology of Shandong Province, Shandong Normal University, Jinan, Shandong 250014, China

2State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, China

*These authors have contributed equally to this work

Correspondence to:

Jun Zhou, email: junzhou@sdnu.edu.cn

Dengwen Li, email: dwli@nankai.edu.cn

Keywords: microtubule, EB1, phosphorylation, CLIP-170, p150glued

Received: October 11, 2016     Accepted: November 24, 2016     Published: December 25, 2016

ABSTRACT

Phosphorylation of end-binding protein 1 (EB1), a key member of microtubule plus end-tracking proteins (+TIPs), by apoptosis signal-regulating kinase 1 (ASK1) has been demonstrated to promote the stability of astral microtubules during mitosis by stimulating the binding of EB1 to microtubule plus ends. However, the roles of other members of the +TIPs family in ASK1/EB1-mediated regulation of astral microtubules are unknown. Herein, we show that ASK1-mediated phosphorylation of EB1 enhances the localization of cytoplasmic linker protein 170 (CLIP-170) and p150glued to the plus ends of astral microtubules. Depletion of ASK1 or expression of phospho-deficient or phospho-mimetic EB1 mutants results in changes in the levels of plus-end localized CLIP-170 or p150glued. Mechanistic studies reveal that EB1 phosphorylation promotes its interactions with CLIP-170 and p150glued, thereby recruiting these +TIPs to microtubules. Structural analysis suggests that serine-40 is the primary phosphorylation site on EB1 that exerts these effects. Together, these findings provide novel insight into the molecular mechanisms that regulate the interactions of EB1 with other +TIPs.


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