MBP Interacts with PIP2 at the Oligodendroglial Cell Membrane: The Role of Phosphoinositides in the Interaction of Myelin Basic Protein with the Oligodendroglial Cell Membrane - Couverture souple

Nawaz, Schanila

 
9783838120799: MBP Interacts with PIP2 at the Oligodendroglial Cell Membrane: The Role of Phosphoinositides in the Interaction of Myelin Basic Protein with the Oligodendroglial Cell Membrane
Couverture souple
ISBN 10 : 3838120795 ISBN 13 : 9783838120799
Editeur : Südwestdeutscher Verlag für Hochschulschriften, 2011

Synopsis

The only protein known to be essential for myelin formation and compaction in the central nervous system is myelin basic protein (MBP). The association of MBP as a positively-charged protein with negatively charged membranes is crucial for myelination, but the mechanisms by which MBP associates with the myelin membrane remains elusive. Here I demonstrate that the signaling lipid PIP2 is important for the stable association of MBP with cellular membranes. This association is lost upon specific decrease of membrane charges through selective hydrolyzation of PIP2 levels or through elevated intracellular Ca2+ levels. Further experiments implicate that one putative PIP2 binding domain of MBP lies within the exon-1 encoded region. The relevance of this protein-lipid interaction was demonstrated for the corpus callosum of mice, after decreasing membrane surface charges in acute brain slices. Here, PIP2 hydrolysis led to the loss of myelin compaction. The results demonstrate that PIP2 plays an important role in MBP association to the plasma membrane. These findings provide a novel link between phosphoinositol metabolism and MBP function in oligodendrocytes in development and disease.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

The only protein known to be essential for myelin formation and compaction in the central nervous system is myelin basic protein (MBP). The association of MBP as a positively-charged protein with negatively charged membranes is crucial for myelination, but the mechanisms by which MBP associates with the myelin membrane remains elusive. Here I demonstrate that the signaling lipid PIP2 is important for the stable association of MBP with cellular membranes. This association is lost upon specific decrease of membrane charges through selective hydrolyzation of PIP2 levels or through elevated intracellular Ca2+ levels. Further experiments implicate that one putative PIP2 binding domain of MBP lies within the exon-1 encoded region. The relevance of this protein-lipid interaction was demonstrated for the corpus callosum of mice, after decreasing membrane surface charges in acute brain slices. Here, PIP2 hydrolysis led to the loss of myelin compaction. The results demonstrate that PIP2 plays an important role in MBP association to the plasma membrane. These findings provide a novel link between phosphoinositol metabolism and MBP function in oligodendrocytes in development and disease.

Biographie de l'auteur

Schanila Nawaz completed her PhD in the field of Neuroscience in January 2009 at the Max Planck Institute for Experimental Medicine in Göttingen, which was followed by a short postdoc period, in the Biophysics department of the University of Göttingen. She has an undergraduate training in biotechnology from the University of Stuttgart.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
Südwestdeutscher Verlag für Hochschulschriften
Date d'édition
2011
Langue
anglais
ISBN 10 
3838120795
ISBN 13 
9783838120799
Reliure
Broché
Nombre de pages
104
Coordonnées du fabricant
non disponible
Personne responsable
info@bod.de
info@bod.de

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