Alternative processing of the sarco/endoplasmic reticulum Ca(2+)-ATPase transcripts during muscle differentiation is a specifically regulated process.
Expression of the muscle-specific 2a isoform of the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA2) requires activation of an otherwise inefficient splice process at the 3'-end of the primary gene transcript. We provide evidence that SERCA2 splicing is a specifically regulated process, rather than the result of an increase in general splice efficiency or a decrease in polyadenylation efficiency at the 5'-most polyadenylation site. This is indicated by the fact that changes in general splice and polyadenylation efficiency, as observed during B-cell maturation, did not affect SERCA2 splicing. Furthermore, expression and overexpression studies did not support the hypothesis that changes in the level of the alternative splice factor ASF/SF2 or other arginine and serine rich proteins are sufficient to obtain the regulation of muscle- and neuronal-specific splicing.
Van den Bosch
L
L
Laboratory of Physiology, University of Leuven, Belgium.
Mertens
L
L
Cavaloc
Y
Y
Peterson
M
M
Wuytack
F
F
Eggermont
J
J
D017398:Alternative Splicing; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000235:genetics* / Q000378:metabolism; D002454:Cell Differentiation; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D051379:Mice; D009132:Muscles / Q000166:cytology / Q000201:enzymology*; D009687:Nuclear Proteins / Q000378:metabolism; D016601:RNA-Binding Proteins; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D000068103:Serine-Arginine Splicing Factors
D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; D000068103:Serine-Arginine Splicing Factors; D000252:Calcium-Transporting ATPases