检索结果-南通市图书馆

NECAB family of neuronal calcium-binding proteins in health and disease

Neural Regeneration Research 2025年第5期20卷 1236-1243页

作者： Diones Bueno Michael K.E.Schafer Sudena Wang Michael J.Schmeisser axel methner Institute for Molecular Medicine University Medical Center of the Johannes Gutenberg-UniversityMainzGermany Department of Anesthesiology University Medical Center of the Johannes Gutenberg-UniversityMainzGermany Institute of Anatomy University Medical Center of the Johannes Gutenberg-UniversityMainzGermany

The N-terminal EF-hand calcium-binding proteins 1–3(NECAB1–3) constitute a family of predominantly neuronal proteins characterized by the presence of at least one EF-hand calcium-binding domain and a functionally less well characterized C-terminal antibiotic biosynthesis monooxygenase domain. All three family members were initially discovered due to their interactions with other proteins. NECAB1 associates with synaptotagmin-1, a critical neuronal protein involved in membrane trafficking and synaptic vesicle exocytosis. NECAB2 interacts with predominantly striatal G-protein-coupled receptors, while NECAB3 partners with amyloid-β A4 precursor protein-binding family A members 2 and 3, key regulators of amyloid-β production. This demonstrates the capacity of the family for interactions with various classes of proteins. NECAB proteins exhibit distinct subcellular localizations: NECAB1 is found in the nucleus and cytosol, NECAB2 resides in endosomes and the plasma membrane, and NECAB3 is present in the endoplasmic reticulum and Golgi apparatus. The antibiotic biosynthesis monooxygenase domain, an evolutionarily ancient component, is akin to atypical heme oxygenases in prokaryotes but is not wellcharacterized in vertebrates. Prokaryotic antibiotic biosynthesis monooxygenase domains typically form dimers, suggesting that calcium-mediated conformational changes in NECAB proteins may induce antibiotic biosynthesis monooxygenase domain dimerization, potentially activating some enzymatic properties. However, the substrate for this enzymatic activity remains uncertain. Alternatively, calcium-mediated conformational changes might influence protein interactions or the subcellular localization of NECAB proteins by controlling the availability of protein–protein interaction domains situated between the EF hands and the antibiotic biosynthesis monooxygenase domain. This review summarizes what is known about genomic organization, tissue expression, intracellular localization, interac

关键词： calcium EF hand mitochondria nervous system signal transduction

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

糖蛋白激素LGR6的结构分析及其表达细胞株的建立

引用

南通医学院学报 2000年第1期20卷 3-5页

作者：徐立 axel methner Rainer Reinscheid 南通医学院生物化学教研室南通226001 德国汉堡大学细胞生化与临床神经生物学研究所

L GR6是新近分离出来的糖蛋白激素受体家族的新成员 ,对分离出来的全长 c DNA及其编码的蛋白质序列初步分析结果显示 ,该受体属于富含亮氨酸重复序列的 G-蛋白偶联受体。c DNA编码一个 977个氨基酸组成的多肽链 ,没有信号肽 ,跨膜区域长... 详细信息

L GR6是新近分离出来的糖蛋白激素受体家族的新成员 ,对分离出来的全长 c DNA及其编码的蛋白质序列初步分析结果显示 ,该受体属于富含亮氨酸重复序列的 G-蛋白偶联受体。c DNA编码一个 977个氨基酸组成的多肽链 ,没有信号肽 ,跨膜区域长为 2 64个氨基酸 ,受体的胞外区域含有 16个 LRR。组织分布的研究显示 ,该受体广泛表达于人体各组织 ,但骨骼肌中没有检测到。该受体在蛋白水平上与 L GR5有 5 1%的同源性。为进一步研究受体的功能 ,我们利用脂质体 DAC-3 0转染 HEK2 93细胞 ,建立了稳定表达 L GR6的细胞株 ,用于今后的研究 ,包括天然配基的分离。

关键词：糖蛋白激素 LRG6 结构分析表达细胞株建立

来源：

维普期刊数据库

同方期刊数据库评论