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

Ran, Jie; Yong, Luo; Zhang, Yijun; Yang, Yang; Chen, Miao; Liu, Min; Li, Dengwen; Zhou, Jun

doi:10.18632/oncotarget.14222

Cited by 14 publications

(13 citation statements)

References 34 publications

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“…Depletion of EB1 decreased Met localization to the cell cortex in response to HGF (Figure C). EB1 depletion or dephosphorylation also results in CLIP‐170 delocalization from MTs (Figure S1C,D) . Hence the observed effects of EB1 KD on Met localization could be mediated through CLIP‐170.…”

Section: Resultsmentioning

confidence: 87%

“…EB1 depletion or dephosphorylation also results in CLIP-170 delocalization from MTs (Figure S1C,D). 38,39 Hence the observed effects of EB1 KD on Met localization could be mediated through CLIP-170. KD of CLIP-170, but not other +TIP binding proteins, such as IQ motif containing GTPase activating protein 1 (IQGAP1) or P150Glued, 31 decreased Met localization to the cell cortex in response to HGF ( Figures 1C and S1C,D) and this was rescued by the re-expression of a nontargetable CLIP-170 expression construct ( Figures 1C and S1E).…”

mentioning

confidence: 97%

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CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

Zaoui

Duhamel

Parachoniak

et al. 2019

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Endocytic sorting of activated receptor tyrosine kinases (RTKs), alternating between recycling and degradative processes, controls signal duration, location and surface complement of RTKs. The microtubule (MT) plus‐end tracking proteins (+TIPs) play essential roles in various cellular activities including translocation of intracellular cargo. However, mechanisms through which RTKs recycle back to the plasma membrane following internalization in response to ligand remain poorly understood. We report that net outward‐directed movement of endocytic vesicles containing the hepatocyte growth factor (HGF) Met RTK, requires recruitment of the +TIP, CLIP‐170, as well as the association of CLIP‐170 to MT plus‐ends. In response to HGF, entry of Met into Rab4‐positive endosomes results in Golgi‐localized γ‐ear‐containing Arf‐binding protein 3 (GGA3) and CLIP‐170 recruitment to an activated Met RTK complex. We conclude that CLIP‐170 co‐ordinates the recycling and the transport of Met‐positive endocytic vesicles to plus‐ends of MTs towards the cell cortex, including the plasma membrane and the lamellipodia, thereby promoting cell migration.

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Section: Resultsmentioning

confidence: 87%

mentioning

confidence: 97%

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

Zaoui

Duhamel

Parachoniak

et al. 2019

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“…To visualize the MT plus ends, we performed MT plus end-binding protein EB1 staining in HeLa cells 19 – 21 . Our data showed that EB1 tracked MT plus end of spindle MTs and astral MTs connected to the cell cortex in scramble cells.…”

Section: Resultsmentioning

confidence: 99%

Palladin is a novel microtubule-associated protein responsible for spindle orientation

Zhang

Chen

Liu

et al. 2017

Sci Rep

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Mitotic spindles, which consist of microtubules (MTs) and associated proteins, play critical roles in controlling cell division and maintaining tissue homeostasis. The orientation of the mitotic spindle is closely related with the duration of mitosis. However, the molecular mechanism in regulating the orientation of the mitotic spindles is largely undefined. In this study, we found that Palladin is a novel MT-associated protein and regulator of spindle orientation, which maintains proper spindle orientation by stabilizing astral MTs. Palladin depletion distorted spindle orientation, prolonged the metaphase, and impaired proliferation of HeLa cells. Results showed that Palladin depletion-induced spindle misorientation and astral MT instability could be rescued by constitutively active AKT1 or dominant negative GSK3β. Our findings revealed that Palladin regulates spindle orientation and mitotic progression mainly through the AKT1–GSK3β pathway.

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“…The control siRNA (5′-CGUACGCGGAAUACUUCGA-3′) and ASK1 siRNAs (#1: 5′-GCACUCCU-UCAUCGAGCU-3′; #2: 5′-GGUAUACAUGAGUGGAAUU-3′) were synthesized by Ribo Bio. Mammalian expression plasmids for GFP-EB1 were constructed by PCR using the pEGFP-N1 vector as described previously [ 31 ].…”

Section: Methodsmentioning

confidence: 99%

EB1 phosphorylation mediates the functions of ASK1 in pancreatic cancer development

Gao

Yong

et al. 2017

Oncotarget

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Pancreatic cancer has a poor prognosis due to its rapid rate of metastasis and frequent late-stage diagnosis. An improved understanding of the molecular mechanisms underlying this disease is urgently needed to promote the development of improved diagnostic tools and more effective therapies. Apoptosis signal-regulating kinase 1 (ASK1) has been shown to be overexpressed in pancreatic cancer and to promote the proliferation of pancreatic cancer cells in a kinase activity-dependent manner. However, the molecular mechanisms by which ASK1 promotes cell proliferation remain to be elucidated. In this study, we report that the phosphorylation of end-binding protein 1 (EB1) at threonine 206 (pT206-EB1), which is catalyzed by ASK1, is increased in pancreatic cancer tissues. We further find that the level of pT206-EB1 correlates with that of ASK1 in cancer tissues. Additionally, ASK1 localizes to spindle poles, and knockdown of ASK1 results in the formation of multipolar spindles. Moreover, we show that depletion of ASK1 or disruption of EB1 phosphorylation inhibits spindle microtubule dynamics in pancreatic cancer cells. Collectively, these findings suggest that EB1 phosphorylation mediates the functions of ASK1 in pancreatic cancer development.

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

Cited by 14 publications

References 34 publications

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

Palladin is a novel microtubule-associated protein responsible for spindle orientation

EB1 phosphorylation mediates the functions of ASK1 in pancreatic cancer development

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