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Phosphorylation of microtubule-associated protein SB401 from Solanum berthaultii Regulates Its Effect on microtubules

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Journal of Integrative Plant Biology 2009年第3期51卷 235-242页

作者： Bao-Quan Liu Lifeng Jin Lei Zhu Jiejie Li Shuli Huang Ming Yuan State Key Laboratory of Plant Physiology and Biochemistry Department of Plant Sciences College of Biological Sciences China Agricultural University Beijing 100094 China Department of Biological Engineering College of Life Sciences Dalian Nationalities University Dalian 116600 China

We reported previously that the protein SB401 from Solanum berthaultii binds to and bundles both microtubules and F-actin. In the current study, we investigated the regulation of SB401 activity by its phosphorylation. Our experimental results showed that the phosphorylation of SB401 by casein kinase II （CKII） downregulates the activities of SB401, namely the bundling of microtubules and enhancement of the polymerization of tubulin. However, phosphorylation of SB401 had no observable effect on its bundling of F-actin. Further investigation using extract of potato pollen indicated that a CKIl-like kinase may exist in potato pollen. Antibodies against CKII alpha recognized specifically a major band from the pollen extract and the pollen extract was able to phosphorylate the SB401 protein in vitro. The CKIl-like kinase showed a similar ability to downregulate the bundling of microtubules. Our experiments demonstrated that phosphorylation plays an important role in the regulation of SB401 activity. We propose that this phosphorylation may regulate the effects of SB401 on microtubules and the actin cytoskeleton.

关键词： F-actin microtubule-associated protein microtubules phosphorylation Solanum berthaultii.

Pathological and physiological functional cross-talks ofα-synuclein and tau in the central nervous system

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Neural Regeneration Research 2024年第4期19卷 855-862页

作者： Mingyue Jin Shengming Wang Xiaodie Gao Zhenyou Zou Shinji Hirotsune Liyuan Sun Guangxi Key Laboratory of Brain and Cognitive Neuroscience Guilin Medical University Department of Genetic Disease Research Osaka Metropolitan University Graduate School of Medicine Department of Scientific Research Brain Hospital of Guangxi Zhuang Autonomous Region

α-Synuclein and tau are abundant multifunctional brain proteins that are mainly expressed in the presynaptic and axonal compartments of neurons,*** works have revealed that intracellular deposition ofα-synuclein and/or tau causes many neurodegenerative disorders,including Alzheimer’s disease and Parkinson’s *** intense investigation,the normal physiological functions and roles ofα-synuclein and tau are still unclear,owing to the fact that mice with knockout of either of these proteins do not present apparent ***,the co-occurrence ofα-synuclein and tau aggregates was found in post-mortem brains with synucleinopathies and tauopathies,some of which share similarities in clinical ***,the direct interaction ofα-synuclein with tau is considered to promote the fibrillization of each of the proteins in vitro and in *** the other hand,our recent findings have revealed thatα-synuclein and tau are cooperatively involved in brain development in a stage-dependent *** findings indicate strong cross-talk between the two proteins in physiology and *** this review,we provide a summary of the recent findings on the functional roles ofα-synuclein and tau in the physiological conditions and pathogenesis of neurodegenerative diseases.A deep understanding of the interplay betweenα-synuclein and tau in physiological and pathological conditions might provide novel targets for clinical diagnosis and therapeutic strategies to treat neurodegenerative diseases.

关键词： alpha-synuclein microtubule-associated protein neurodegenerative disease tau

Dynamics of cooperative transport by multiple kinesin motors and diffusing microtubule-associated proteins

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Communications in Theoretical Physics 2022年第10期74卷 136-149页

作者： Yao Wang Yu-Ru Liu Peng-Ye Wang Ping Xie Key Laboratory of Soft Matter Physics Institute of PhysicsChinese Academy of SciencesBeijing 100190China School of Physical Sciences University of Chinese Academy of SciencesBeijing 100049China

In eukaryote cells,cargos are often transported cooperatively by kinesin motors and nonmotor microtubule-associated proteins(MAPs).The prior in vitro experimental data showed that the velocity of the cargo transported by kinesin motors and Ndc80(a member of MAP)proteins of truncated coiled-coil stalks decreases sensitively with the increase of the ratio of Ndc80 to motor ***,the underlying mechanism of Ndc80 affecting sensitively the cooperative cargo transport by kinesin motors is *** understand the mechanism,here we study numerically the cooperative cargo transport by kinesin motors and Ndc80 *** results showed that for the case of the motors and Ndc80 proteins with truncated short stalks,as used in the experiments,the calculated results reproduce quantitatively the prior experimental *** mechanism of the cargo velocity decreasing sensitively with the ratio of Ndc80 to motor number is *** contrast,for the case of the motors and Ndc80 proteins with full-length long stalks,the velocity of the cargo decreases slowly with the increase in the ratio of Ndc80 to kinesin *** results thus give an explanation of why the kinesin motors working in the cell have long stalks.

关键词： intracellular transport molecular motor kinesin microtubule-associated protein Ndc80

Micro RNA-9 promotes the neuronal differentiation of rat bone marrow mesenchymal stem cells by activating autophagy

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Neural Regeneration Research 2015年第2期10卷 314-320页

作者： Guang-yu Zhang Jun Wang Yan-jie Jia Rui Han Ping Li Deng-na Zhu Rehabilitation and Treatment Center for Children with Cerebral Palsy of Henan Province the Third Affiliated Hospital of Zhengzhou University Department of Neurology the First Affiliated Hospital of Zhengzhou University Department of Pediatrics the Third Affiliated Hospital of Zhengzhou University

MicroRNA-9 （miR-9） has been shown to promote the differentiation of bone marrow mesen-chymal stem cells into neuronal cells, but the precise mechanism is unclear. Our previous study conifrmed that increased autophagic activity improved the efifciency of neuronal differentiation in bone marrow mesenchymal stem cells. Accumulating evidence reveals that miRNAs adjust the autophagic pathways. This study used miR-9-1 lentiviral vector and miR-9-1 inhibitor to modulate the expression level of miR-9. Autophagic activity and neuronal differentiation were measured by the number of light chain-3 （LC3）-positive dots, the ratio of LC3-II/LC3, and the expression levels of the neuronal markers enolase and microtubule-associated protein 2. Re-sults showed that LC3-positive dots, the ratio of LC3-II/LC3, and expression of neuron speciifc enolase and microtubule-associated protein 2 increased in the miR-9＋ group. The above results suggest that autophagic activity increased and bone marrow mesenchymal stem cells were prone to differentiate into neuronal cells when miR-9 was overexpressed, demonstrating that miR-9 can promote neuronal differentiation by increasing autophagic activity.

关键词： nerve regeneration,microRNA-9 bone marrow mesenchymal stem cells differentiation neuron-like cells autophagy neuron specific enolase microtubule-associated protein LC3 neural regeneration

Overexpression of Tau Rescues Nogo-66-Induced Neurite Outgrowth Inhibition In Vitro

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Neuroscience Bulletin 2016年第6期32卷 577-584页

作者： Yu-Chao Zuo Hong-Lian Li Nan-Xiang Xiong Jian-Ying Shen Yi-Zhi Huang Peng Fu Hong-Yang Zhao Department of Neurosurgery Union Hospital.Tongji Medical CollegeHuazhong University of Science and Technology Department of Neurosurgery The First Affiliated Hospital of Zhengzhou University Department of Anatomy Tongji Medical CollegeHuazhong University of Science and Technology

Abstract Nogo-66 plays a central role in the myelin- mediated inhibition of neurite outgrowth. Tau is a micro- tubule-associated protein involved in microtubule assembly and stabilization. It remains unverified whether tau inter- acts directly with growth factor receptors, or engages in cross-talk with regeneration inhibitors like Nogo-66. Here, we report that plasmid overexpression of tau significantly elevated the protein levels of total tau, phosphorylated tau, and microtubule-affinity regulating kinase （MARK）. Nogo- 66 transiently elevated the total tau protein level and per- sistently reduced the level of p-s262 tau （tau phosphory- lated at serine 262）, whereas it had little influence on the level of p-T205 tau （tau phosphorylated at threonine 205）. Nogo-66 significantly decreased the protein level of MARK. Hymenialdisine, an inhibitor of MARK, signifi- cantly reduced the level of p-S262 tau. Overexpression of tau rescued the Nogo-66-induced inhibition of neurite outgrowth in neuroblastoma cortical neurons. However, 2a （N2a） cells and primary concomitant inhibition ofMARK abolished the rescue of neurite outgrowth by tan in N2a cells. We conclude that dephosphorylation of tau at S262 is able to regulate Nogo-66 signaling, and that overexpression of tau can rescue the Nogo-66-induced inhibition of neurite outgrowth in vitro.

关键词： Neurite outgrowth Myelin inhibitor microtubule-associated protein Phosphorylation

Alp7-Mtol and Alpl4 synergize to promote interphase microtubule regrowth from the nuclear envelope

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Journal of Molecular Cell Biology 2019年第11期11卷 944-955页

作者： Wenyue Liu Fan Zheng Yucai Wang Chuanhai Fu Division of Molecular and Cell Biophysics Hefei National Science Center for Physical SciencesUniversity of Science and Technology of ChinaHefeiChina Chinese Academy of Sciences Center for Excellence in Molecular Cell Sciences School of Life SciencesUniversity of Science and Technology of ChinaHefeiChina Anhui Key Laboratory for Cellular Dynamics and Chemical Biology University of Science and Technology of ChinaHefeiChina School of Life Sciences University of Science and Technology of ChinaHefeiChina

microtubules grow not only from the centrosome but also from various noncentrosomal microtubule-organizing centers(MTOCs),including the nuclear envelope(NE)and pre-existing *** evolutionarily conserved proteins Mtol/CDK5RAP2 and Alpl4/TOG/XMAP215 have been shown to be involved in promoting microtubule ***,it has remained elusive as to how the microtubule nucleation promoting factors are specified to various noncentrosomal MTOCs,particularly the NE,and how these proteins coordinate to organize microtubule ***,we demonstrate that in the fission yeast Schizosaccharomyces pombe,efficient interphase microtubule growth from the NE requires Alp7/TACC,Alpl4/TOG/XMAP215,and Mtol/*** absence of Alp7,A lp l4 t or Mtol compromises microtubule regrowth on the NE in cells undergoing microtubule *** further demonstrate that Alp7 and Mtol interdependently localize to the NE in cells without microtubules and that A lp l4 localizes to the NE in an Alp7 and Mtol-dependent *** Mtol to the NE in cells lacking Alp7 partially restores microtubule number and the efficiency of microtubule generation from the ***,our study delineates that Alp7,A lpl4,and Mtol work in concert to regulate interphase microtubule regrowth on the NE.

关键词： microtubule microtubule nucleation nuclear envelope microtubule-associated protein fission yeast