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Dynamic Events in Myosin and Actin and Their Function

肌球蛋白和肌动蛋白的动态事件及其功能

基本信息

批准号：
7535191
负责人：
EMIL REISLER
金额：
$ 50.27万
依托单位：
UNIVERSITY OF CALIFORNIA LOS ANGELES
依托单位国家：
美国
项目类别：
财政年份：
1978
资助国家：
美国
起止时间：
1978-07-01 至 2010-11-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7535191
关键词：
ATP-G-actin Actin-Binding Protein Actins Actomyosin Amino Acids Binding Binding Proteins Cell physiology Cells Chemotaxis Cleaved cell Collaborations Complement Complex Computer Simulation Crystallization Cysteine Deoxyribonuclease I Development Digestion Electron Microscopy Eukaryotic Cell Event F-Actin Family Filament Fluorescence Resonance Energy Transfer Gel Gelsolin Generations Goals Grant Growth Head Hydroxyl Radical Immune Kinetics Knowledge Life Maps Mass Spectrum Analysis Measurement Measures Methods Microfilaments Modeling Molecular Conformation Motion Motor Muscle Contraction Mutagenesis Myosin ATPase Neoplasm Metastasis Organism Peptides Pharmaceutical Preparations Play Process Property Proteins Proteolysis Regulation Research Research Personnel Role Site Solutions Solvents Staging Structure Takeda brand of pioglitazone hydrochloride Testing Therapeutic Intervention Work Wound Healing Yeasts actin-S1 blocking factor cell motility cofilin crosslink dimer improved insight light scattering mutant novel oxidation pathogen polymerization programs research study sedimentation velocity single molecule synchrotron radiation tool

项目摘要

Cell motility and force generation are fundamental features of living organisms. Actin, one of the most conserved and aboundant proteins in eukaryotic cells, plays a key role in these processes. The long-term goal of this research is to provide detailed understanding of structure and dynamic events that underlie force generation by actomyosin and the remodeling of actin filaments for cellular needs. This goal will be pursued through a combination of x-ray structure determination of actin oligomers and their complexes, and solution studies probing actin filaments structure, dynamics, interactions, and fuction via cross-linking, kinetic, spectroscopic, electron microscopy, and mutagenesis methods. The specific aims of the three projects of this study are: I, (i-iv) To map by radiolysis, mass spectrometry, cleavage, and cross-linking methods the interaction sites of actin and cofilin, and actin and myosin in strongly and weakly bound complexes. II. (i-iii) To crystallize and solve the structures of actin dimers, tetramers, and their complexes with cofilin, gelsolin fragments, capping proteins, and myosin heads (S1). . (i-iii) To stabilize the early forms of actin filaments and assess the role of anti-parallel dimers in the growth of filament branches; (iy) To test by spectroscopic and mutagenesis methods the structure of the DNase I binding loop on actin; (v) To determine the mechanism of actin filament severing by cofilin and gelsolin, and to clarify the activation of cofilin function by the actin interacting protein Aip1. Detailed understanding of the structure, dynamics and interactions of actin should clarify the mechanism of its function in muscle contraction and in cellular processes, such as wound healing, cancer metastasis, chemotaxis of immune cells and host-pathogen interactions. Ultimately, this understanding should help in the development of therapeutic interventions as drugs that influence actin interactions are discovered.

细胞运动和产生力是生物体的基本特征。肌动蛋白是最

项目成果

期刊论文数量（92）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Immunochemical probing of the N-terminal segment on actin: the polymerization reaction.

肌动蛋白 N 末端片段的免疫化学探测：聚合反应。

DOI：
10.1021/bi00465a024
发表时间：
1990
期刊：
Biochemistry
影响因子：
2.9
作者：
DasGupta,G;White,J;Phillips,M;Bulinski,JC;Reisler,E
通讯作者：
Reisler,E

Locking the hydrophobic loop 262-274 to G-actin surface by a disulfide bridge prevents filament formation.

通过二硫桥将疏水环262-274锁定至G-肌动蛋白表面可防止细丝形成。

DOI：
10.1021/bi020205f
发表时间：
2002
期刊：
Biochemistry
影响因子：
2.9
作者：
Shvetsov,Alexander;Musib,Runa;Phillips,Martin;Rubenstein,PeterA;Reisler,Emil
通讯作者：
Reisler,Emil

Thin filament regulation and ionic interactions between the N-terminal region in actin and troponin.

肌动蛋白和肌钙蛋白 N 端区域之间的细丝调节和离子相互作用。