Juxtanodin is an intrinsically disordered F-actin-binding protein.

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. Ensemble optimization analysis of the data suggested also the presence of more compact forms of juxtanodin. The C terminus was a strict requirement for co-sedimentation of juxtanodin with microfilaments, but juxtanodin had only mild effects on actin polymerization. The disordered nature of juxtanodin may predict functions as a protein interaction hub, although F-actin is its only currently known binding partner.

Citation

Salla Ruskamo, Maryna Chukhlieb, Juha Vahokoski, Saligram Prabhakar Bhargav, Fengyi Liang, Inari Kursula, Petri Kursula. Juxtanodin is an intrinsically disordered F-actin-binding protein. Scientific reports. 2012;2:899

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PMID: 23198089

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