G 蛋白对磷脂酶 Cbeta 的激活-猫眼课题宝

G 蛋白对磷脂酶 Cbeta 的激活

批准号：

8588934

负责人：

Suzanne F Scarlata

金额：

$31.4万

依托单位：

STATE UNIVERSITY NEW YORK STONY BROOK

依托单位国家：

美国

项目类别：

财政年份：

1995

资助国家：

美国

项目状态：

已结题

起止时间：

1995-08-01 至 2015-11-30

来源：

https://reporter.nih.gov/project-details/8588934

关键词：

Affect Attenuated Automobile Driving Binding Calcium Calcium Signaling Cancer-Predisposing Gene Cancerous Caveolae Cell Nucleus Cell Proliferation Cell membrane Cells Cessation of life Complex Cultured Cells Cytosol Data Disease Down-Regulation Enzymes Family Fluorescence GTP-Binding Proteins Gamma synuclein Guanosine Triphosphate Guanosine Triphosphate Phosphohydrolases Heterotrimeric GTP-Binding Proteins Hormones Hydrolysis In Vitro Lead Life Link Lipids Measures Mediating Mediator of activation protein Membrane Methods Molecular Nerve Degeneration Neurodegenerative Disorders Neurons Neurotransmitters Nuclear Pathway interactions Peptides Phenotype Phosphatidylinositol 4,5-Diphosphate Phospholipase Phospholipase C Play Population Protein Family Protein Kinase C Proteins RNA RNA Binding RNA Interference Reagent Regulation Role Signal Transduction Small Interfering RNA Therapeutic Tissues Work alpha synuclein base cell growth regulation cell motility cellular imaging fluorescence imaging malignant breast neoplasm novel overexpression prevent protein activation public health relevance receptor coupling response stoichiometry synuclein

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DESCRIPTION (provided by applicant): P.I. S. Scarlata Phospholipase C-b (PLC?) enzymes are activated by G proteins in response to agents such as hormones and neurotransmitters. PLC? activity causes an increase in intracellular calcium which ultimately leads to profound changes in the cell. Our lab has focused on the mechanism through which G proteins activate PLC? on the molecular level. However, in cultured cells, we find additional and unexpected mechanisms of regulation. First, membrane domains called caveolae can control the duration of PLC? activation by selectively sequestering G protein activators. 1 - In AIM 1, we will use live cell imaging and state of the art fluorescence methods to determine the mechanisms through which caveolae prolongs PLC? - mediated calcium signals and directs signals along specific cellular pathways. 2- We have found that PLCb localizes to the nucleus and cytosol as well as the plasma membrane where its G protein activators are found. We have identified a novel protein partner of PLC? translin-associated protein X (TRAX). TRAX and its partner translin are major components of the siRNA machinery regulating the cellular levels of proteins. In AIM 2, we will determine the ability of TRAX to deliver PLC? from the nucleus to the plasma membrane upon G protein activation. In parallel, we will determine whether PLC affects translin-TRAX function. 3- The ability of PLC? to generate signals depends on its cellular concentration. We have found that the synucleins can binds to and stabilize PLC? in cells. Alpha-synuclein (AS) is a small unfolded protein of unknown function and is a major component of neurodegenerative plaques. The presence of AS greatly increases PLC? levels, and we find that down-regulation of PLC??causes AS aggregation. Also, gamma- synuclein (GS), the protein encoded by the breast cancer susceptibility gene 1, appears to increase PLCb -mediated migration and cell invasiveness thereby promoting breast cancer. In AIM 3 we will better define PLC? - synuclein interactions and develop reagents that prevent AS aggregation and reduce GS-induced breast cancer phenotype.

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