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中国神经科学学会第九届全国学术会议暨第五次会员代表大会

作者： Cai-Yun DENG~(**),Xiao-Hui XU~(**),Yang LIU,Tong WANG,Zhen-Ge LUO~* Institute of Neuroscience and State Key Laboratory of Neuroscience,Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences,Shanghai 200031,China

＜正＞The formation of axons and dendrites and maintenance of the neuron’s vastly expanded surface require the continuous addition of new *** axon extension,the coordination of membrane traffic,adhesion to extracellular substrate,and reorganization of the cytoskeleton at the peripheral region of the growth cone mediate the protrusive activity of the axon growth *** we have found the involvement of Rab10 in directional membrane insertion of plasmalemmal precursor vesicles（PPV） during neuronal *** the mechanism of Rab10 action remains *** we report that the myristoylated alanine-rich C kinase substrate（MARCKS） interacts with Rab10 and mediates fusion of PPV to the plasma ***-regulation of MARCKs using siRNA against MARCKS abrogated polarized distribution of Rab10 and prevented neuronal ***, blockade of the interaction between Rab10 and MARCKS by over-expressing the MARCKS domain that mediated the RablO-MARCKS binding abolished membrane fusion of PPVs,which were labeled with BODIPY-ceramide. membrane fusion of PPVs was also measured by analyzing the TIRF（Internal Reflection Fluorescence） signals of pHluorin-tagged receptors of axon growth promoting factors - TrkB for brain-derived neurotrophic factor（BDNF） and IGFR for insulin like factor 1（IGF-1）.We found that down-regulation of MARCKS or blocking its interaction with Rab10 inhibited the TIRF ***,blocking the interaction between Rab10 and MARCKS inhibited axon growth in vitro and in ***,Rab10 interaction with MARCKS mediates fusion of PPV with the plasma membrane,a process required for axonal growth.

关键词： MARCKS Rab10 plasmalemmal precursor vesicle axonal growth fusion membrane insertion

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How does a β-barrel integral membrane protein insert into the membrane？

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Protein & Cell 2016年第7期7卷 471-477页

作者： Xuejun C. Zhang Lei Han National Laboratory of Macromolecules National Center of Protein Science- Beijing Institute of Biophysics Chinese Academyof Sciences Beijing 100101 China

Integral membrane proteins （MPs） are categorized into two major groups： transmembrane （TM） α-helical bundles and β-barrels （Cymer et al., 2014）. Both types of structures permit the backbones of their peptides to fulfill their hydro- gen-bonding potential in a lipid-bilayer environment. The thermal stability of a typical β-barrel MP is usually much higher than that of a helical MP. Thus, β-barrel MPs are able to withstand near boiling-temperatures during purification （Han et al., 2016）, compared with the typical melting tem- peratures of 50℃ or lower for a-helical TM proteins. In fact, unfolding a β-barrel MP in a single-molecule assay typically requires multiple steps, each of which requires a force of 100-300 pN （Thoma et al., 2015）. Considering the thickness of the membrane as well as the multiple steps, unfolding one mole of β-barrel MP molecules would require -103 kJ of energy （equivalent to 400 RT or energy from hydrolyzing 20-30 moles of ATP）. Such high thermal stability is consid- ered to be the sole source of the energy that drives the folding of β-barrel MPs （Fleming, 2015）.China

关键词： Outer membrane Lipid Bilayer Substrate Peptide Periplasmic Space membrane insertion

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Interaction of SynaptotagminⅠ with Phospholipid membrane: A Monolayer Study

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Tsinghua Science and Technology 2002年第4期7卷 379-383页

作者：贺雨虹隋森芳 State Key Laboratory of Biomembrane Department of Biological Sciences and BiotechnologyTsinghua University Beijing 100084 China

Synaptotagmin Ⅰ(sytⅠ) is an abundant integral membrane protein of the synaptic vesicle and the C2A domain is an important functional domain in the cytoplasmic part of sytⅠ. C2A prefers to interact with plasmic membranes of neuron cells in vivo and such interaction is closely related to the sytⅠ physiological function as a Ca 2+ sensor in the Ca 2+ regulated neurotransmitter release. However, the interaction nature between C2A and phospholipids is not well understood. Monolayers at an air/water interface were used to study the interaction between C2A and a phospholipid membrane. The results show that C2A preferentially inserts into the negatively charged phosphatidylserine monolayer and Ca 2+ ions are required for the interaction. Electrostatic force is mostly responsible for the insertion of C2A into dipalmitoyl phosphatidylserine monolayers.

关键词： synaptotagminⅠ membrane insertion phospholipid monolayers lipid/protein interaction

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Concerted recruitment of CaMKIIα and caveolin-1 drives ligand-induced membrane delivery of functional P2X3 receptor

Concerted recruitment of CaMKIIα and caveolin-1 drives liga...

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中国神经科学学会第十届全国学术会议

作者： Xu-Qiao CHEN Yan-Qing ZHONG Jing-Xiang ZHU Yan WANG XU ZHANG Lan BAO State Key Laboratory of Cell Biology Institute of Biochemistry and Cell BiologyShanghai Institutes for Biological SciencesChinese Academy of Sciences Institute of Neuroscience and State Key Laboratory of Neuroscience Shanghai Institutes for Biological SciencesChinese Academy of Sciences

Accumulated evidence shows that P2X receptor plays a crucial role in sensory processing and *** assembly and trafficking of P2X receptor are important for its function in primary sensory *** an important inflammation mediator,ATP is released from various cell types around primary sensory neurons,especially in pathological pain *** have previously reported that ATP potentiated the endocytosis and retrograde axonal transport of P2X receptor in a form of "signaling endosome" in primary sensory ***,we showed that ATP also dramatically promoted membrane delivery of bom exogenous and endogenous P2X receptors,α,β-MeATP induced the P2X receptor-mediated Ca influx,which further activated Ca/calmodulin-dependent protein kinase IIα(CaMKIIα).The N terminus of P2X receptor was responsible for binding to CaMKIIα,whereas Thr388 in the C terminus was phosphorylated by CaMKIIα,indicating that CaMKIIα regulates the membrane insertion of P2X receptor in a tertiary structure-dependent *** Thr388 phosphorylation increased the binding of P2X receptor with caveolin-1,while the P2X mutant which lost ability to bind to caveolin-1 displayed a very low level of membrane *** down of caveolin-1 abrogated the α,β-MeATP-induced membrane insertion of P2X ***,α,β-MeATP drove the CaMKIIα-mediated membrane coinsertion of P2X receptor which coassembles with P2X *** ATP-increased P2X receptor on the cell membrane facilitated the P2X receptor-mediated current and signal ***,our data indicate that CaMKIIα and caveolin-1 cooperate to drive the ligand-induced membrane delivery of P2X receptor,and may provide a mechanism of P2X receptor sensitization in pain development.

关键词： P2X3 receptor ATP membrane insertion CaMKIIa caveolin-1 P2X2 receptor

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