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神经元蛋白NP25与丝状肌动蛋白相互作用。

Neuronal protein NP25 interacts with F-actin.

作者信息

Mori Kenji, Muto Yoshinori, Kokuzawa Jouji, Yoshioka Takashi, Yoshimura Shinichi, Iwama Toru, Okano Yukio, Sakai Noboru

机构信息

Department of Neurosurgery, Gifu University School of Medicine, Tsukasa-machi, Gifu, Japan.

出版信息

Neurosci Res. 2004 Apr;48(4):439-46. doi: 10.1016/j.neures.2003.12.012.

Abstract

Neuronal protein NP25 is a neuron-specific protein present in highly differentiated neural cells, but its functional properties have not been well characterized. NP25 shows high amino acid sequence homology with the smooth muscle cell cytoskeleton-associated proteins, SM22, mp20, and calponin. To gain an insight into the biological functions of NP25, we first examined its subcellular localization in the human neuroblastoma cell line, SK-N-SH. NP25 diffusely distributed in the cytoplasm and fiber-like staining was also observed. It showed that NP25 co-localized with F-actin on stress fibers. A co-sedimentation assay demonstrated that NP25 bound to filamentous actin. Further investigations using fluorescence resonance energy transfer (FRET) technique revealed intracellular binding of NP25 and actin. The significance of the interaction between NP25 and F-actin is discussed.

摘要

神经元蛋白NP25是一种存在于高度分化神经细胞中的神经元特异性蛋白,但其功能特性尚未得到充分表征。NP25与平滑肌细胞细胞骨架相关蛋白SM22、mp20和钙调蛋白具有高度的氨基酸序列同源性。为了深入了解NP25的生物学功能,我们首先在人神经母细胞瘤细胞系SK-N-SH中检测了其亚细胞定位。NP25在细胞质中呈弥漫性分布,同时也观察到纤维状染色。结果表明,NP25与应激纤维上的F-肌动蛋白共定位。共沉降分析表明NP25与丝状肌动蛋白结合。使用荧光共振能量转移(FRET)技术的进一步研究揭示了NP25与肌动蛋白在细胞内的结合。本文讨论了NP25与F-肌动蛋白相互作用的意义。

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