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Salla Ruskamo, Maryna Chukhlieb, Juha Vahokoski, Saligram Prabhakar Bhargav, Fengyi Liang, Inari Kursula, Petri Kursula
Juxtanodin, also called ermin, is an F-actin-binding protein expressed by oligodendrocytes, the myelin-forming cells of the central nervous system. While juxtanodin carries a short conserved F-actin-binding segment at its C terminus, it otherwise shares no similarity with known protein sequences. We carried out a structural characterization of recombinant juxtanodin in solution. Juxtanodin turned out to be intrinsically disordered, as evidenced by conventional and synchrotron radiation CD spectroscopy. Small-angle X-ray scattering indicated that juxtanodin is a monomeric, highly elongated, unfolded molecule...
2012: Scientific Reports
Tao Wang, Lintao Jia, Guodong Yang, Shaoping Ji, Libo Yao, Bin Zhang
Juxtanodin (JN) is a cytoskeleton-related oligodendrocyte-specific gene, and its underlying mechanism still needs detailed exploration. In this study, we tested whether a 1.9 kb fragment from the 5'-flanking region of JN is sufficient to specifically deliver the gene expression in oligodendrocytes. By reporter assay, we found that the 1.9 kb fragment specifically activated in C6 cells, which is further upregulated by ATRA-induced oligodendrocyte lineage differentiation. Bioinformatics study revealed that Nkx2...
April 2011: Molecular and Cellular Biochemistry
Jun Meng, Wenhao Xia, Junhong Tang, Bor Luen Tang, Fengyi Liang
In the vertebrate central nervous system, maturation of oligodendrocytes is accompanied by a dramatic transformation of cell morphology. Juxtanodin (JN) is an actin cytoskeleton-related oligodendroglial protein that promotes arborization of cultured oligodendrocytes. We performed in vitro and in culture experiments to further elucidate the biochemical effects, molecular interactions, and activity regulation of JN. Pulldown and co-sedimentation assays confirmed JN binding to filamentous but not globular beta-actin largely through a C-terminal domain of 14 amino acid residues...
September 10, 2010: Journal of Biological Chemistry
J Tang, J Tang, E-A Ling, Y Wu, F Liang
In the CNS, juxtanodin (JN) is an actin-binding oligodendroglial protein that functions to promote differentiation of the host cells during postnatal development. In other tissues, JN expression and function remain unknown. We surveyed rat peripheral nerve, skeletal muscle and various epithelial tissues using immunoblotting and light-microscopic immunohistochemistry, and found prominent JN expression only in the olfactory epithelium (OE). Confocal and immunoelectron microscopy further revealed specific JN expression in the glia-like sustentacular cells and in the ductal cells of Bowman's glands...
June 16, 2009: Neuroscience
Wenbo Li, Bin Zhang, Junhong Tang, Qiong Cao, Yajun Wu, Chun Wu, Jing Guo, Eng-Ang Ling, Fengyi Liang
Silent information regulator-2 (SIR2) proteins regulate lifespan of diverse organisms, but their distribution and roles in the CNS remain unclear. Here, we show that sirtuin 2 (SIRT2), a mammalian SIR2 homolog, is an oligodendroglial cytoplasmic protein and localized to the outer and juxtanodal loops in the myelin sheath. Among cytoplasmic proteins of OLN-93 oligodendrocytes, alpha-tubulin was the main substrate of SIRT2 deacetylase. In cultured primary oligodendrocyte precursors (OLPs), SIRT2 emergence accompanied elevated alpha-tubulin acetylation and OLP differentiation into the prematurity stage...
March 7, 2007: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
Bin Zhang, Qiong Cao, Anchen Guo, Haiying Chu, Yee Gek Chan, Jan Paul Buschdorf, Boon Chuan Low, Eng Ang Ling, Fengyi Liang
In the process of screening cell-type-specific genes, we identified juxtanodin (JN), an oligodendroglial protein featuring a putative C-terminal actin-binding domain. At the cellular level, JN in the rat CNS colocalized with 2',3'-cyclic nucleotide-3'-phosphodiesterase (CNPase), a cytoskeleton-related oligodendroglial protein. In the myelin sheath, JN was found mainly in the abaxon and the lateral few terminal loops. Its apposition to the myelinated axon, through the latter, defined an axonal subregion, herewith termed juxtanode, at the Ranvier node-paranode junction...
August 9, 2005: Proceedings of the National Academy of Sciences of the United States of America
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