Abstract:
:Little is known about how adhesion molecules on APCs accumulate at immunological synapses. We show here that ICAM-1 on APCs is continuously internalized and rapidly recycled back to the interface after antigen-priming T-cell contact. The internalization rate is high in APCs, including Raji B cells and dendritic cells, but low in endothelial cells. Internalization is significantly reduced by inhibitors of Na(+)/H(+) exchangers (NHEs), suggesting that members of the NHE-family regulate this process. Once internalized, ICAM-1 is co-localized with MHC class II in the polarized recycling compartment. Surprisingly, not only ICAM-1, but also MHC class II, is targeted to the immunological synapse through LFA-1-dependent adhesion. Cytosolic ICAM-1 is highly mobile and forms a tubular structure. Inhibitors of microtubule or actin polymerization can reduce ICAM-1 mobility, and thereby block accumulation at immunological synapses. Membrane ICAM-1 also moves to the T-cell contact zone, presumably through an active, cytoskeleton-dependent mechanism. Collectively, these results demonstrate that ICAM-1 can be transported to the immunological synapse through the recycling compartment. Furthermore, the high-affinity state of LFA-1 on T cells is critical to induce targeted movements of both ICAM-1 and MHC class II to the immunological synapse on APCs.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Jo JH,Kwon MS,Choi HO,Oh HM,Kim HJ,Jun CDdoi
10.1002/jcb.22798subject
Has Abstractpub_date
2010-12-01 00:00:00pages
1125-37issue
5eissn
0730-2312issn
1097-4644journal_volume
111pub_type
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