UNDERSTANDING THE ROLES OF SMALL GTPASES IN CELL GROWTH REGULATION
UNDERSTANDING THE ROLES OF SMALL GTPASES IN CELL GROWTH REGULATION
批准号:
7955176
负责人:
RICHARD A. CERIONE
金额:
$0.86万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2009
资助国家:
美国
项目状态:
已结题
起止时间:
2009-04-01 至 2010-03-31
关键词:
Cell Cycle ProgressionCell Differentiation processCell ShapeCellular biologyComputer Retrieval of Information on Scientific Projects DatabaseDifferentiation and GrowthFundingGTP BindingGTP-Binding ProteinsGeneticGoalsGrantGuanosine Triphosphate PhosphohydrolasesHydrolysisInstitutionMediatingMonomeric GTP-Binding ProteinsPlayProcessResearchResearch PersonnelResourcesRoleSourceStudy modelsUnited States National Institutes of HealthWorkbasecell growth regulationcell motilityprotein complexresponsestructural biology
中文摘要
这个子项目是众多研究子项目之一
英文摘要
This subproject is one of many research subprojects utilizing the
resources provided by a Center grant funded by NIH/NCRR. The subproject and
investigator (PI) may have received primary funding from another NIH source,
and thus could be represented in other CRISP entries. The institution listed is
for the Center, which is not necessarily the institution for the investigator.
The goal of our research has been to combine structural approaches with cell biology and genetic studies in order to better understand fundamental processes that contribute to the growth and differentiation of cells. The structural work entails two lines of experimental efforts of increasing complexity. The first involves understanding the conformational changes underlying the activation (GTP-binding) and deactivation (GTP hydrolysis) of GTP-binding proteins (GTPases). We have been using Cdc42 and related small GTPases (e.g. RhoC), which play critical roles in coordinating cell cycle progression and proliferation with cell shape changes and cell migration, as models for these studies. A second major line of study is directed toward determining the mechanistic and structural basis for the actions of multi-protein complexes that direct the activation of Cdc42 and mediates its cellular responses.
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