Dynamic Interactions between Intrinsically Disordered Proteins and Curved Membrane Surfaces
本质无序蛋白质与弯曲膜表面之间的动态相互作用
基本信息
- 批准号:10708024
- 负责人:
- 金额:$ 39.44万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2022
- 资助国家:美国
- 起止时间:2022-09-22 至 2027-07-31
- 项目状态:未结题
- 来源:
- 关键词:3-DimensionalAdsorptionAffectBehaviorBindingBiologicalBiophysical ProcessBiophysicsCell physiologyDefectDiseaseEndocytic VesicleEnvironmentEquilibriumFluorescence MicroscopyGoalsHumanKineticsKnowledgeLaboratoriesLiteratureMeasurementMeasuresMembraneMembrane Protein TrafficMissionPhaseProtein EngineeringProteinsProteomePublic HealthResearchResearch Project GrantsSignal TransductionStructureSurfaceSynaptic VesiclesSystemTechniquesTestingThermodynamicsUnited States National Institutes of HealthVisualizationWorkhuman diseaseinterestmalignant neurologic neoplasmsmillisecondnervous system disorderprogramsprotein aggregationprotein structuresensorthree dimensional structuretraffickingtwo-dimensional
项目摘要
Project Summary/Abstract. Intrinsically Disordered Proteins (IDPs) represent approximately 40% of the human
proteome and are implicated in a large number of human diseases, including neurological disorders and cancer.
Therefore, the biological relevance of IDPs has garnered substantial interest over the last decade. IDPs often
interact with curved membranes to form structures that are essential to cellular physiology, such as synaptic and
endocytic vesicles. These interactions are facilitated by membrane curvature sensing. The PI recently discovered
that IDPs are potent sensors of membrane curvature. This discovery is a substantive departure from the
predominant structure-function paradigm, as IDPs lack fixed three-dimensional structure and are often incorrectly
assumed to also lack biophysical functionality. The curvature sensitivity of IDPs, as well as many other types of
proteins, is normally studied at thermodynamic equilibrium. However, membrane-interacting proteins exist in a
dynamic equilibrium between their membrane-bound and membrane-unbound states. It can take minutes to
achieve thermodynamic equilibrium between proteins and membranes, but cellular processes, such as cell
signaling, occur anywhere between milliseconds to seconds. It is clear from this mismatch in timescales that
when thermodynamic equilibrium alone is considered, dynamic information that is pertinent to the timescale of
cellular processes is omitted. Little to no literature exists that examines this phenomenon, likely owing to the
difficulty associated with achieving such experimental measurements. Thus, dynamic interactions between
proteins and curved membrane structures are poorly understood. Using their expertise in quantitative
fluorescence microscopy and protein engineering, the goal of the PI's laboratory is to develop and apply
techniques and strategies that will allow for direct visualization and characterization of dynamic interactions
between IDPs and curved membrane structures. The PI's future research program contains 3 overarching
research projects. Work in Project 1 will evaluate the extent to which protein structure influences adsorption and
desorption kinetics, testing the working hypothesis that curved membranes affect various protein structures
differently. Work in Project 2 will evaluate the impact of protein networks on the binding dynamics of IDPs,
answering questions about the influence of protein multivalency on dynamic behavior. Work in Project 3 will
develop experimental techniques and strategies that mimic the intracellular environment, answering questions
about dynamic interactions between IDPs and curved membrane substrates that occur in the presence of two-
dimensional, phase separated protein mixtures on the membrane surface or three-dimensional protein
aggregates in the bulk solution. As previously mentioned, our current understanding of the interactions between
proteins and curved membranes was derived from systems in which the partitioning of proteins was measured
after thermodynamic equilibrium was achieved. In contrast, the proposed work will fill a key gap in existing
knowledge by directly observing and quantifying dynamic interactions between proteins and curved membranes.
项目总结/抽象。内在无序蛋白(IDPs)约占人类的40%
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Wade F Zeno其他文献
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{{ truncateString('Wade F Zeno', 18)}}的其他基金
Dynamic Interactions between Intrinsically Disordered Proteins and Curved Membrane Surfaces
本质无序蛋白质与弯曲膜表面之间的动态相互作用
- 批准号:
10502133 - 财政年份:2022
- 资助金额:
$ 39.44万 - 项目类别:
Intrinsically Disordered Proteins as Sensors of Membrane Curvature
本质上无序的蛋白质作为膜曲率的传感器
- 批准号:
9788761 - 财政年份:2018
- 资助金额:
$ 39.44万 - 项目类别:
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