Abstract:
:Various multisubunit receptors of the immune system share similarities in structure and induce closely related signal transduction pathways upon ligand binding. Examples include the T cell antigen receptor (TCR), the B cell antigen receptor (BCR), and the high-affinity receptor for immunoglobulin E (Fc epsilon RI). Although these receptors are devoid of intrinsic kinase activity, they can associate with a similar array of intracellular kinases, phosphatases and other signaling molecules. Furthermore, these receptor complexes all form an association with the cytoskeletal matrix. In this review, we compare the structural and functional characteristics of the TCR, BCR and Fc epsilon RI. We examine the role of the cytoskeleton in regulating receptor-mediated signal transduction, as analyzed in other well-characterized receptors, including the epidermal growth factor receptor and integrin receptors. On the basis of this evidence, we review the current data depicting a cytoskeletal association for multisubunit immune system receptors and explore the potential bearing of this interaction on signaling function.
journal_name
Immunol Resjournal_title
Immunologic researchauthors
Caplan S,Baniyash Mdoi
10.1007/BF02918171subject
Has Abstractpub_date
1995-01-01 00:00:00pages
98-118issue
2eissn
0257-277Xissn
1559-0755journal_volume
14pub_type
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