T cell CD3-zeta eta heterodimer expression and coupling to phosphoinositide hydrolysis.
The T cell antigen receptor consists of an antigen-binding heterodimer that is noncovalently associated with at least five CD3 subunits (gamma, delta, epsilon, zeta, and eta). The CD3-zeta chains are either disulfide-linked homodimers ( CD3-zeta 2) or disulfide-linked heterodimers with eta ( CD3-zeta eta). Variants of a murine antigen-specific T cell hybridoma that express normal amounts of CD3-zeta 2 but decreased amounts of CD3-zeta eta were isolated. When activated, the parental cell line increased both phosphatidylinositol hydrolysis and serine-specific protein kinase activity to a much greater extent than the variants. In contrast, the activation of a tyrosine-specific kinase after stimulation with a cross-linking antibody to CD3 was similar among these cells. There was a positive linear relation between the expression of CD3-zeta eta and phosphoinositide hydrolysis stimulated by the TCR, suggesting a differential coupling of the T cell alpha beta heterodimer to signal transduction mechanisms due to alpha beta association with either CD3-zeta 2 or CD3-zeta eta.[1]References
- T cell CD3-zeta eta heterodimer expression and coupling to phosphoinositide hydrolysis. Merćep, M., Bonifacino, J.S., Garcia-Morales, P., Samelson, L.E., Klausner, R.D., Ashwell, J.D. Science (1988) [Pubmed]
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