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NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids Dedicated to Professor Chaohui Ye on the occasion of his 80th birthday

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Magnetic Resonance Letters 2022年第4期2卷 205-213页

作者： Yunyan Li Yong Liu Huiqin Zhang Zhen Wang Maosen Ruan Jiarong Wang Jing Yang Bo Wu Junfeng Wang High Magnetic Field Laboratory CAS Key Laboratory of High Magnetic Field and Ion Beam Physical BiologyHefei Institutes of Physical ScienceChinese Academy of SciencesHefei230031China University of Science and Technology of China Hefei230026China Institutes of Physical Science and Information Technology Anhui UniversityHefei230601China Anhui University Hefei230039China

Fibroblast growth factor receptors(FGFRs)play an important role in the regulation of cell proliferation,migration and differentiation,while the juxtamembrane domain(JMD)of FGFRs is the key in mediating these transmembrane signal transduction ***,we expressed and purified the JMD(398K-470R)of FGFR1 with the presence of transmembrane domain(377I-397Y).The results from nuclear magnetic resonance(NMR)chemical shift analysis demonstrate that the main structure of JMD is ***,the N-terminus of JMD was observed to form a short a-helix upon introducing negatively charged lipid 1,2-dioleoyl-sn-glycero-3-phospho-L-serine(DOPS)into its membrane mimic ***,the N-terminus of JMD interacts with FRS2a,which is a substrate 2a of ***,we propose a model that FGFR1-JMD may interact with FRS2a and negatively charged lipids *** study provides a new understanding on the role of the JMD of FGFRs.

关键词： Fibroblast growth factor receptors(FGFRs) Juxtamembrane domain FGFR substrate 2a Negatively charged lipid Secondary structure transition Nuclear magnetic resonance(NMR) protein-lipid interaction

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Binding of Mono, Bi and Tridomain proteins to Zwitterionic and Anionic Vesicles： Asymmetric Location of Anionic Phospholipids in Mixed Zwitterionic/Anionic Vesicles and Cooperative Binding

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Journal of Life Sciences 2011年第3期5卷 167-181页

作者： Francisco Torrens Gloria Castellano Institute for Molecular Science University of Valencia Valencia E-46071 Spain Energesis Chair of Interdisciplinary Technology Saint Vincent Martyr Catholic University of Valencia Valencia E-46003 Spain

Lysozyme, myoglobin and BSA were used as models of globular proteins covering a wide range of pl. The purpose is to extend the studies to anionic lipid bilayers. Electrostatics is studied in cationic protein adsorption to zwitterionic PC and anionic mixed PC/PG SUVs. protein adsorption is investigated in SUVs along with changes of fluorescence emission spectra. Partition coefficients and cooperativity parameters are calculated. At pl binding obtains maximum while at lower or higher pHs binding decreases. In Gouy-Chapman formalism activity coefficient goes with square charge, which deviations indicate asymmetric location of anionic phospholipid in the inner leaflet, in mixed SUVs for lysozyme- and myoglobin-PC/PG systems, in agreement with experiments and molecular dynamics simulations. Vesicles bind myoglobin anti-cooperatively while lysozyme-BSA cooperativitivey. A model is proposed for both, which composes two protein sub-layers with different structures and properties. Hill coefficient reflects subunit cooperativity of bi and tridomain proteins.

关键词： protein-lipid interaction sigmoid adsorption isotherm transbilayer asymmetry anionic phospholipid asymmetric location cooperative binding hill plot.

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