Retargeting of viral glycoproteins into a non-exporting compartment during the myogenic differentiation of rat L6 cells

We have analysed protein trafficking during the differentiation of rat L6 myoblasts into myotubes. Different proteins were found to lose different amounts of their processing by the Golgi apparatus during the myogenic differentiation, indicating that they were transported to this organelle with diff...

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Bibliographic Details
Published in:	Cell and tissue research Vol. 308; no. 3; pp. 381 - 390
Main Authors:	Kaisto, Tuula, Luukela, Veera, Birr, Elli, Metsikkö, Kalervo
Format:	Journal Article
Language:	English
Published:	Germany Springer Nature B.V 01-06-2002
Subjects:	Animals Brefeldin A - pharmacology Cell Compartmentation - physiology Cell Line Cytoplasm - metabolism Endoplasmic Reticulum - metabolism Fluorescent Antibody Technique Glycosylphosphatidylinositols - metabolism Golgi Apparatus - metabolism Membrane Glycoproteins - pharmacokinetics Myoblasts - cytology Myoblasts - metabolism Protein Synthesis Inhibitors - pharmacology Protein Transport - drug effects Protein Transport - physiology Rats Temperature Viral Envelope Proteins - pharmacokinetics Viral Fusion Proteins - pharmacokinetics
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Summary:	We have analysed protein trafficking during the differentiation of rat L6 myoblasts into myotubes. Different proteins were found to lose different amounts of their processing by the Golgi apparatus during the myogenic differentiation, indicating that they were transported to this organelle with differing efficiencies. In order to investigate the destination of the nonprocessed glycoproteins we analysed the behaviour of vesicular stomatitis virus (VSV) and Semliki Forest virus glycoproteins in the presence of Brefeldin A, which returns the enzymes of the Golgi apparatus to the ER. Such experiments indicated that during myogenesis a fraction of both glycoproteins was shunted into a compartment that did not participate recycling with the Golgi apparatus. Immunofluorescence studies with the mutant VSV tsO45 G protein suggested that this compartment was diffusively distributed. We investigated whether the cytoplasmic tail had a role in the myogenic transport modulation by analysing the behaviour of recombinant VSV G proteins. Exchanging the cytoplasmic tail or the tail plus the membrane anchor had no effect, suggesting that the luminal portion was responsible for the diverted transport. Taken together, the results suggest that during the myogenesis of L6 myoblasts, varying fractions of different viral glycoproteins were sorted from the ER into a specific compartment that did not recycle with the Golgi apparatus.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0302-766X 1432-0878
DOI:	10.1007/s00441-002-0556-5