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CD28 stimulation regulates its association with N ‐ethylmaleimide‐sensitive fusion protein and other proteins involved in vesicle sorting
Author(s) -
Heller Manfred,
Watts Julian D.,
Aebersold Ruedi
Publication year - 2001
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200101)1:1<70::aid-prot70>3.0.co;2-p
Subject(s) - cd28 , jurkat cells , microbiology and biotechnology , biology , protein targeting , stimulation , fusion protein , t cell , chemistry , membrane protein , biochemistry , immunology , immune system , endocrinology , recombinant dna , gene , membrane
CD28 delivers a co‐stimulatory signal for Tcell 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.