TY - JOUR
T1 - Structure and expression of a novel compact myelin protein - Small VCP-interacting protein (SVIP)
AU - Wu, Jiawen
AU - Peng, Dungeng
AU - Voehler, Markus
AU - Sanders, Charles R.
AU - Li, Jun
N1 - Funding Information:
Authors wish to thank Dr. Shengyun Fang for his generous gifts of antibodies. We also thank Dr. Xuebao Zhang, Ms. Sezgi Arpag and Audra Hamilton for their technical assistance. This research is supported by grants from NINDS (R21NS081364 and R01NS066927 to J.L.; RO1 NS058815 to C.S.), NIH (SIG #1S-10RR025677-01), and VA (B6243R to J.L.). This material is the result of work partially supported with resources and the use of facilities at the VA Tennessee Valley Healthcare System.
PY - 2013/10/11
Y1 - 2013/10/11
N2 - 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.
AB - 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.
KW - Compact myelin
KW - Intrinsically disordered protein
KW - Myelin basic protein
KW - Protein-membrane interaction
KW - Small VCP-interacting protein
KW - Valosin containing protein
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U2 - 10.1016/j.bbrc.2013.09.056
DO - 10.1016/j.bbrc.2013.09.056
M3 - Article
C2 - 24055875
AN - SCOPUS:84885369790
VL - 440
SP - 173
EP - 178
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -