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Title: The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal

Abstract

Highlights: Black-Right-Pointing-Pointer Full-length 21.5-kDa MBP isoform is translocated to the nucleus. Black-Right-Pointing-Pointer We hypothesized that the exon-II-encoded sequence contained the NLS. Black-Right-Pointing-Pointer We mutated this sequence in RFP-tagged constructs and transfected N19-cells. Black-Right-Pointing-Pointer Abolition of two key positively-charged residues resulted in loss of nuclear-trafficking. Black-Right-Pointing-Pointer The 21.5-kDa isoform of classic MBP contains a non-traditional PY-NLS. -- Abstract: The predominant 18.5-kDa classic myelin basic protein (MBP) is mainly responsible for compaction of the myelin sheath in the central nervous system, but is multifunctional, having numerous interactions with Ca{sup 2+}-calmodulin, actin, tubulin, and SH3-domains, and can tether these proteins to a lipid membrane in vitro. The full-length 21.5-kDa MBP isoform has an additional 26 residues encoded by exon-II of the classic gene, which causes it to be trafficked to the nucleus of oligodendrocytes (OLGs). We have performed site-directed mutagenesis of selected residues within this segment in red fluorescent protein (RFP)-tagged constructs, which were then transfected into the immortalized N19-OLG cell line to view protein localization using epifluorescence microscopy. We found that 21.5-kDa MBP contains two non-traditional PY-nuclear-localization signals, and that arginine and lysine residues within these motifs were involved in subcellular trafficking of this protein to the nucleus, where it may havemore » functional roles during myelinogenesis.« less

Authors:
;  [1];  [2];  [1]
  1. Molecular and Cellular Biology, University of Guelph, Guelph, Ontario (Canada)
  2. Molecular Structure and Function, Research Institute, Hospital for Sick Children, and Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario (Canada)
Publication Date:
OSTI Identifier:
22207892
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 422; Journal Issue: 4; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACTIN; ARGININE; CALMODULIN; CENTRAL NERVOUS SYSTEM; FLUORESCENCE; LYSINE; MYELIN; SIGNALS

Citation Formats

Smith, Graham S.T., Seymour, Lauren V., Boggs, Joan M., and Harauz, George, E-mail: gharauz@uoguelph.ca. The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal. United States: N. p., 2012. Web. doi:10.1016/J.BBRC.2012.05.051.
Smith, Graham S.T., Seymour, Lauren V., Boggs, Joan M., & Harauz, George, E-mail: gharauz@uoguelph.ca. The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal. United States. doi:10.1016/J.BBRC.2012.05.051.
Smith, Graham S.T., Seymour, Lauren V., Boggs, Joan M., and Harauz, George, E-mail: gharauz@uoguelph.ca. Fri . "The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal". United States. doi:10.1016/J.BBRC.2012.05.051.
@article{osti_22207892,
title = {The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal},
author = {Smith, Graham S.T. and Seymour, Lauren V. and Boggs, Joan M. and Harauz, George, E-mail: gharauz@uoguelph.ca},
abstractNote = {Highlights: Black-Right-Pointing-Pointer Full-length 21.5-kDa MBP isoform is translocated to the nucleus. Black-Right-Pointing-Pointer We hypothesized that the exon-II-encoded sequence contained the NLS. Black-Right-Pointing-Pointer We mutated this sequence in RFP-tagged constructs and transfected N19-cells. Black-Right-Pointing-Pointer Abolition of two key positively-charged residues resulted in loss of nuclear-trafficking. Black-Right-Pointing-Pointer The 21.5-kDa isoform of classic MBP contains a non-traditional PY-NLS. -- Abstract: The predominant 18.5-kDa classic myelin basic protein (MBP) is mainly responsible for compaction of the myelin sheath in the central nervous system, but is multifunctional, having numerous interactions with Ca{sup 2+}-calmodulin, actin, tubulin, and SH3-domains, and can tether these proteins to a lipid membrane in vitro. The full-length 21.5-kDa MBP isoform has an additional 26 residues encoded by exon-II of the classic gene, which causes it to be trafficked to the nucleus of oligodendrocytes (OLGs). We have performed site-directed mutagenesis of selected residues within this segment in red fluorescent protein (RFP)-tagged constructs, which were then transfected into the immortalized N19-OLG cell line to view protein localization using epifluorescence microscopy. We found that 21.5-kDa MBP contains two non-traditional PY-nuclear-localization signals, and that arginine and lysine residues within these motifs were involved in subcellular trafficking of this protein to the nucleus, where it may have functional roles during myelinogenesis.},
doi = {10.1016/J.BBRC.2012.05.051},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 422,
place = {United States},
year = {2012},
month = {6}
}