A point mutation in CD28 distinguishes proliferative signals from survival signals View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-04

AUTHORS

Klaus Okkenhaug, Linda Wu, Kristine M. Garza, Jose La Rose, Wilson Khoo, Bernhard Odermatt, Tak W. Mak, Pamela S. Ohashi, Robert Rottapel

ABSTRACT

Upon interaction with its ligand, B7, CD28 becomes phosphorylated on tyrosines. One tyrosine in particular (Y170 in mouse CD28, Y173 in human CD28) has received much attention. This is because it permits CD28 to recruit SH2-containing signaling molecules, including phosphoinositide 3 kinase, Grb2 and Gads. Using mice we employed a transgenic approach to express a tyrosine→phenylalanine mutant form of CD28 that uncouples these SH2-mediated interactions from CD28. The CD28 mutant is unable to up-regulate expression of the prosurvival protein Bcl-xL, rendering the T cells more susceptible to radiation-induced death. Nonetheless, this mutated form of CD28 still prevents the induction of anergy and promotes T cell proliferation, interleukin 2 secretion and B cell help. Thus, we describe a single point mutation within the CD28 cytoplasmic domain that uncouples signals required for proliferation and survival. More... »

PAGES

325-332

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/86327

DOI

http://dx.doi.org/10.1038/86327

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016438100

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11276203


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