Structure and expression of a novel compact myelin protein - Small VCP-interacting protein (SVIP)

Jiawen Wu, Dungeng Peng, Markus Voehler, Charles R. Sanders, Jun Li

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


SVIP (small p97/VCP-interacting protein) was initially identified as one of many cofactors regulating the valosin containing protein (VCP), an AAA+ ATPase involved in endoplasmic-reticulum-associated protein degradation (ERAD). Our previous study showed that SVIP is expressed exclusively in the nervous system. In the present study, SVIP and VCP were seen to be co-localized in neuronal cell bodies. Interestingly, we also observed that SVIP co-localizes with myelin basic protein (MBP) in compact myelin, where VCP was absent. Furthermore, using nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopic measurements, we determined that SVIP is an intrinsically disordered protein (IDP). However, upon binding to the surface of membranes containing a net negative charge, the helical content of SVIP increases dramatically. These findings provide structural insight into interactions between SVIP and myelin membranes.

Original languageEnglish (US)
Pages (from-to)173-178
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Oct 11 2013


  • Compact myelin
  • Intrinsically disordered protein
  • Myelin basic protein
  • Protein-membrane interaction
  • Small VCP-interacting protein
  • Valosin containing protein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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