Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.4049/jimmunol.164.10.5287

Type

Journal article

Journal

J Immunol

Publication Date

15/05/2000

Volume

164

Pages

5287 - 5295

Keywords

Alternative Splicing, Animals, Arginine, COS Cells, Exons, Humans, Leukocyte Common Antigens, Nuclear Proteins, Phosphoproteins, Protein Isoforms, Protein Structure, Tertiary, RNA Precursors, RNA-Binding Proteins, Serine, Serine-Arginine Splicing Factors, T-Lymphocytes, Transfection