Document Detail


Classic 18.5- and 21.5-kDa myelin basic protein isoforms associate with cytoskeletal and SH3-domain proteins in the immortalized N19-oligodendroglial cell line stimulated by phorbol ester and IGF-1.
MedLine Citation:
PMID:  22249765     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The 18.5-kDa classic myelin basic protein (MBP) is an intrinsically disordered protein arising from the Golli (Genes of Oligodendrocyte Lineage) gene complex and is responsible for compaction of the myelin sheath in the central nervous system. This MBP splice isoform also has a plethora of post-translational modifications including phosphorylation, deimination, methylation, and deamidation, that reduce its overall net charge and alter its protein and lipid associations within oligodendrocytes (OLGs). It was originally thought that MBP was simply a structural component of myelin; however, additional investigations have demonstrated that MBP is multi-functional, having numerous protein-protein interactions with Ca²⁺-calmodulin, actin, tubulin, and proteins with SH3-domains, and it can tether these proteins to a lipid membrane in vitro. Here, we have examined cytoskeletal interactions of classic 18.5-kDa MBP, in vivo, using early developmental N19-OLGs transfected with fluorescently-tagged MBP, actin, tubulin, and zonula occludens 1 (ZO-1). We show that MBP redistributes to distinct 'membrane-ruffled' regions of the plasma membrane where it co-localizes with actin and tubulin, and with the SH3-domain-containing proteins cortactin and ZO-1, when stimulated with PMA, a potent activator of the protein kinase C pathway. Moreover, using phospho-specific antibody staining, we show an increase in phosphorylated Thr98 MBP (human sequence numbering) in membrane-ruffled OLGs. Previously, Thr98 phosphorylation of MBP has been shown to affect its conformation, interactions with other proteins, and tethering of other proteins to the membrane in vitro. Here, MBP and actin were also co-localized in new focal adhesion contacts induced by IGF-1 stimulation in cells grown on laminin-2. This study supports a role for classic MBP isoforms in cytoskeletal and other protein-protein interactions during membrane and cytoskeletal remodeling in OLGs.
Authors:
Graham S T Smith; Lopamudra Homchaudhuri; Joan M Boggs; George Harauz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-01-17
Journal Detail:
Title:  Neurochemical research     Volume:  37     ISSN:  1573-6903     ISO Abbreviation:  Neurochem. Res.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-05-03     Completed Date:  2012-08-31     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  7613461     Medline TA:  Neurochem Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1277-95     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Biology, University of Guelph, 50 Stone Road East, Guelph, ON N1G 2W1, Canada.
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MeSH Terms
Descriptor/Qualifier:
Cell Line
Cell Membrane / metabolism*
Cortactin / metabolism
Focal Adhesions
Humans
Insulin-Like Growth Factor I / pharmacology*
Microscopy, Fluorescence
Myelin Basic Protein / chemistry,  metabolism*
Oligodendroglia / drug effects,  metabolism*
Protein Isoforms / chemistry,  metabolism
Protein Processing, Post-Translational
Tetradecanoylphorbol Acetate / pharmacology*
Tubulin / metabolism
src Homology Domains
Grant Support
ID/Acronym/Agency:
86483//Canadian Institutes of Health Research; MOP 86483//Canadian Institutes of Health Research
Chemical
Reg. No./Substance:
0/Cortactin; 0/Myelin Basic Protein; 0/Protein Isoforms; 0/Tubulin; 16561-29-8/Tetradecanoylphorbol Acetate; 67763-96-6/Insulin-Like Growth Factor I
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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