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Peptidergic granules in trigeminal ganglion neurons

三叉神经节神经元中的肽能颗粒

基本信息

批准号：
7630547
负责人：
Jacqueline A Sobota
金额：
$ 2.88万
依托单位：
UNIVERSITY OF CONNECTICUT SCH OF MED/DNT
依托单位国家：
美国
项目类别：
财政年份：
2005
资助国家：
美国
起止时间：
2005-07-10 至 2009-06-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7630547
关键词：
Adenoviruses Antibodies Biochemical Biotinylation Cell Fractionation Cell surface Confocal Microscopy Cytoplasmic Granules Degradation Pathway Dense Core Vesicle Endocytosis Endoplasmic Reticulum Event Fluorescence Recovery After Photobleaching Fluorescent Probes Goals Homeostasis Immune Sera Integral Membrane Protein Kinetics Life Membrane Membrane Protein Traffic Membrane Proteins Methods Mixed Function Oxygenases Morphology Mutation Nervous system structure Neurons Neuropeptides Optics Pathway interactions Peptides Phosphorylation Phosphotransferases Process Proteins RNA Interference Recombinants Recycling Role Route Secretory Component Secretory Vesicles Stimulus Structure of trigeminal ganglion Testing Virus enhanced green fluorescent protein in vivo insight mutant peptidylglycine alpha-amidating monooxygenase prevent research study time use trafficking

项目摘要

Description (provided by the applicant): Regulated secretion of neuropeptides is essential for maintaining homeostasis within the nervous system. This process relies on the proper assembly of peptide-containing large dense core vesicles (LDCVs, or secretory granules), which in turn requires coordinated machinery to synthesize the LDCV membrane, package soluble contents, and retrieve components for degradation or recycling. Although these trafficking events are critical to function, little is known regarding the biosynthetic or recycling pathways of LDCVs in neurons. The studies proposed will focus on the trafficking of peptidylglycine alpha-amidating monooxygenase (PAM), an integral granule membrane protein known to carry out the last steps in the peptide biosynthetic pathway. The cytosolic domain of PAM contains routing information and is phosphorylated by the kinase PCIP2 at Ser949. This proposal will specifically test the hypothesis that PAM-1 is a dynamic component of secretory membranes in peptidergic neurons of the trigeminal ganglion, and that specific trafficking steps are regulated by phosphorylation at Ser949 by P-CIP2.

描述（由申请人提供）：神经肽的调节分泌对于维持神经系统内的稳态至关重要。该过程依赖于含肽大致密核心囊泡（LDCV 或分泌颗粒）的正确组装，而这又需要协调的机器来合成 LDCV 膜、包装可溶性内容物并回收组分以供降解或回收。尽管这些转运事件对于功能至关重要，但人们对 LDCV 在神经元中的生物合成或回收途径知之甚少。拟议的研究将重点关注肽基甘氨酸α-酰胺化单加氧酶（PAM）的运输，这是一种完整的颗粒膜蛋白，已知执行肽生物合成途径的最后步骤。 PAM 的胞质结构域包含路由信息，并被激酶 PCIP2 在 Ser949 处磷酸化。该提案将专门测试以下假设：PAM-1 是三叉神经节肽能神经元分泌膜的动态成分，并且特定的运输步骤由 P-CIP2 在 Ser949 处的磷酸化来调节。