Regulation of alternative splicing of CD45 by antagonistic effects of SR protein splicing factors.
SourceJournal of Immunology, 164, 10, (2000), pp. 5287-95
Article / Letter to editor
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Cell Biology (UMC)
Journal of Immunology
SubjectThe role of protein-tyrosine phosphatase genes, encoding potential tumor suppressors, in tumor initiation and progression; Role of fatty acid-binding proteins, proteoglycans and ion transport in differentiation and pathology; De rol van submembrane proteine-tyrosine fosfatases potentiële tumor suppressors bij celgroei en differentiatie; De rol van vetzuurbindende eiwitten, proteoglycanen en iontransport bij differentiatie en pathologie
CD45 is a transmembrane glycoprotein possessing tyrosine phosphatase activity, which is involved in cell signaling. CD45 is expressed on the surface of most leukocytes and can be alternatively spliced by the inclusion or skipping of three variable exons (4, 5, and 6 or A, B, and C) to produce up to eight isoforms. In T cells, the splicing pattern of CD45 isoforms changes after activation; naive cells express high m.w. isoforms of CD45 which predominantly express exon A (CD45RA), whereas activated cells lose expression of exon A to form low m.w. isoforms of CD45 including CD45RO. Little is known about the specific factors controlling the switch in CD45 splicing which occurs on activation. In this study, we examined the influence of the SR family of splicing factors, which, like CD45, are expressed in tissue-specific patterns and have been shown to modulate the alternative splicing of a variety of transcripts. We show that specific SR proteins have antagonistic effects on CD45 splicing, leading either to exon inclusion or skipping. Furthermore, we were able to demonstrate specific changes in the SR protein expression pattern during T cell activation.
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