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Ermin oligodendrocytes

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https://www.readbyqxmd.com/read/23198089/juxtanodin-is-an-intrinsically-disordered-f-actin-binding-protein
#1
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
https://www.readbyqxmd.com/read/20934411/human-ermin-hermin-a-new-oligodendrocyte-specific-cytoskeletal-protein-related-to-epileptic-seizure
#2
Tao Wang, Lintao Jia, Bochang Lv, Bei Liu, Wei Wang, Fang Wang, Guodong Yang, Xin Bu, Libo Yao, Bin Zhang
During the maturation of oligodendrocytes, cells are characterized by their morphological changes such as the number of process extensions and sheet-like membranes. This process relies critically on cytoskeleton rearrangement, but the molecular mechanisms underlying this are still unclear. Here, we identify human Ermin (hErmin), a novel cytoskeletal molecule that is expressed exclusively in oligodendrocytes in human brain, as a regulator of cytoskeleton rearrangement. In vitro, full-length hErmin expression, but not its truncated mutants lacking the actin-binding domain, promote arborization of cultured COS-7 cells and induce marked changes in cell morphology...
January 7, 2011: Brain Research
https://www.readbyqxmd.com/read/16421295/ermin-a-myelinating-oligodendrocyte-specific-protein-that-regulates-cell-morphology
#3
COMPARATIVE STUDY
Damian Brockschnieder, Helena Sabanay, Dieter Riethmacher, Elior Peles
Oligodendrocytes form an insulating multilamellar structure of compact myelin around axons, thereby allowing rapid propagation of action potentials. Despite the considerable clinical importance of myelination, little is known about the molecular mechanisms that enable oligodendrocytes to generate their specialized membrane wrapping. Here, we used microarray expression profiling of oligodendrocyte-ablated mutant mice to identify new glial molecules that are involved in CNS myelination. This effort resulted in the identification of Ermin, a novel cytoskeletal molecule that is exclusively expressed by oligodendrocytes...
January 18, 2006: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
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