ORGANIZATION AND FUNCTIONS OF THE NUCLEAR LAMINA

核层的组织和功能

• 批准号: 7957746
• 负责人: Larry R. Gerace
• 金额: $ 0.33万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-01 至 2010-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957746
• 关键词: Biology; C-terminal; Computer Retrieval of Information on Scientific Projects Database; Disease; Excision; Funding; Fungal Genome; Grant; Institution; Lamin Type A; Liver; Molecular; Mus; Mutation; Nuclear Envelope; Nuclear Lamina; Progeria; Proteomics; Research; Research Personnel; Resources; Source; United States National Institutes of Health; base; gain of function; mutant; prevent

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. Hutchinson-Guilford progeria is caused by a mutant form of lamin A that contains an internal deletion in its C-terminal region. This prevents the proteolytic removal of the farnesylated C-terminus of lamin A that normally takes place, and leads to a toxic gain of function. To understand the molecular basis of this disease, we are carrying out proteomic analysis of nuclear envelopes isolated from the livers of mice with mutations that prevent normal removal of the lamin A farnesylated C-terminus.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 Hutchinson-guilford pogeria是由层状A的突变形式引起的，该突变体在其C末端区域包含内部缺失。 这样可以防止通常发生的层粘连蛋白A的蛋白水解去除层粘连的C末端，并导致功能的有毒增益。为了了解该疾病的分子基础，我们正在对从小鼠肝脏中分离出的核信封进行蛋白质组学分析，这些突变可防止正常去除层粘连蛋白a farnesylation farneyl c-termation c-末端。