Abstract:
:CD28 delivers a co-stimulatory signal for T cell antigen receptor induced activation of T cells through a mechanism which remains mostly elusive to date. In order to try and gain insight into CD28 function, we therefore applied state-of-the-art mass spectrometric protein identification technology to the analysis of CD28 immunoprecipitates prepared from Jurkat T cells. We found that N-ethylmaleimide-sensitive fusion protein (NSF) and other proteins with sequence similarities to proteins part of or implicated in vesicular protein sorting pathways, were associated with CD28 in a CD28 stimulation-dependent manner. Furthermore, N-ethylmaleimide treatment abolished the NSF/CD28 interaction completely, and blocked CD28 association with a tyrosine phosphorylated 103 kDa protein in the activated cells. These results are suggestive of a potential model for CD28 co-stimulation regulated by an NSF-catalyzed mechanism.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Heller M,Watts JD,Aebersold Rdoi
10.1002/1615-9861(200101)1:1<70::AID-PROT70>3.0.COsubject
Has Abstractpub_date
2001-01-01 00:00:00pages
70-8issue
1eissn
1615-9853issn
1615-9861journal_volume
1pub_type
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