1. Cell Biology
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Intermediate Filaments: The sweet side of vimentin

  1. Natasha T Snider
  2. Nam-On Ku
  3. M Bishr Omary  Is a corresponding author
  1. University of North Carolina at Chapel Hill, United States
  2. Yonsei University, Republic of Korea
  3. University of Michigan Medical School, United States
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Cite this article as: eLife 2018;7:e35336 doi: 10.7554/eLife.35336
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Glycosylation of a serine residue in the ‘head’ domain of vimentin promotes interactions between vimentin molecules.

A vimentin molecule has three domains: the head, the rod (which is α-helical), and the tail. Tarbet et al. show that the glycosylation of the Ser49 residue in the head domain (indicated by the addition of the yellow square) promotes the formation of vimentin dimers; the glycosylation of Ser34 (not shown) also promotes dimer formation, but to a lesser extent. While the exact details of the dimer formation process remain to be clarified, biochemical evidence suggests that glycosylation mediates interactions between the head domain of one vimentin molecule and either the head or rod domain of a second vimentin molecule, or with assembled vimentin filaments.

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