Multiple splice isoforms of proteolipid M6B in neurons and oligodendrocytes

Proteolipids are abundant integral membrane proteins, initially described as structural proteins of CNS myelin. More recently, two neuronal proteins related to proteolipid protein (PLP), termed M6A and M6B, were identified, suggesting a common function of proteolipids in oligodendrocytes and neurons...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Werner, Hauke (VerfasserIn) , Dimou, Leda (VerfasserIn) , Klugmann, Matthias (VerfasserIn) , Nave, Klaus-Armin (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: December 2001
In: Molecular and cellular neuroscience
Year: 2001, Jahrgang: 18, Heft: 6, Pages: 593-605
ISSN:1095-9327
DOI:10.1006/mcne.2001.1044
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1006/mcne.2001.1044
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S1044743101910449
Volltext
Verfasserangaben:Hauke Werner, Leda Dimou, Matthias Klugmann, Steve Pfeiffer, Klaus-Armin Nave
Beschreibung
Zusammenfassung:Proteolipids are abundant integral membrane proteins, initially described as structural proteins of CNS myelin. More recently, two neuronal proteins related to proteolipid protein (PLP), termed M6A and M6B, were identified, suggesting a common function of proteolipids in oligodendrocytes and neurons. We have analyzed the X-linked M6B gene and discovered an unexpected complexity of protein isoforms. Two promoters and alternative exons yield at least eight M6B proteins and polypeptides, differentially expressed in neurons and oligodendrocytes. Six isoforms are tetraspan membrane proteins that differ by highly conserved amino- and carboxy-terminal domains, termed α, β, ψ, and ω. In MDCK cells, the β-domain of M6B stabilizes tetraspan proteolipids at the cell surface, whereas non-β isoforms are more abundant in intracellular compartments. Cotransfection experiments suggest a physical interaction of M6B and mutant PLP, when retained in the endoplasmic reticulum, that may also contribute to oligodendrocyte dysfunction in Pelizaeus-Merzbacher disease.
Beschreibung:Gesehen am 06.06.2017
Beschreibung:Online Resource
ISSN:1095-9327
DOI:10.1006/mcne.2001.1044