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Distinct Trafficking of Cell Surface and Endosomal TIM-1 to the Immune Synapse

Artikel i vetenskaplig tidskrift
Författare Meriem Echbarthi
M. Zonca
R. Mellwig
Y. Schwab
G. Kaplan
R. H. Dekruyff
P. Roda-Navarro
J. M. Casasnovas
Publicerad i Traffic : the International Journal of Intracellular Transport
Volym 16
Nummer/häfte 11
Sidor 1193-1207
ISSN 1398-9219
Publiceringsår 2015
Publicerad vid Institutionen för kemi och molekylärbiologi
Sidor 1193-1207
Språk en
Länkar dx.doi.org/10.1111/tra.12329
Ämnesord Immune synapse, Microscopy, Protein sorting, Structural immunology, T-cell, TIM family
Ämneskategorier Cell- och molekylärbiologi, Immunologi inom det medicinska området

Sammanfattning

The T cell costimulatory molecule TIM-1 (T cell/transmembrane, mucin and immunoglobulin domain protein 1) sorts mainly to endosomes in lymphoid cells. At difference from the cell surface protein, endosomal TIM-1 translocates to the immune synapse (IS), where it can contribute to antigen-dependent T cell costimulation. TIM-1 ligands increase the amount of cell surface protein, preventing its traffic to the IS. The bipolar sorting of TIM-1 observed during IS formation is determined by differences in its subcellular location, and probably modulates antigen-driven immune responses. The T-cell/transmembrane, mucin and immunoglobulin domain protein 1 (TIM-1) is a phosphatidlyserine (PtdSer) receptor and a T-cell costimulatory molecule linked to the development of atopic diseases. TIM-1 locates preferentially in intracellular compartments. Here we show that in human and mouse lymphoid cells, TIM-1 localizes in different types of endosomes and that its domain structure is important for protein sorting to intracellular vesicles. The BALB/c mouse TIM-1 protein, which has a longer mucin domain, is sorted more efficiently to endosomes than the shorter C57BL/6 variant. High affinity ligands such as PtdSer increase the amount of cell surface TIM-1; the protein also polarizes toward cell contacts with apoptotic cells. The large pool of intracellular TIM-1 translocates to the immune synapse (IS) with the CD3-TCR (T-cell receptor) complex and colocalizes to the central supramolecular activation cluster (cSMAC). In contrast, cell surface TIM-1 does not traffic to the IS, but is located away from it. The bipolar TIM-1 sorting observed during IS formation is determined by differences in its subcellular location, and might modulate antigen-driven immune responses. © 2015 John Wiley & Sons A/S.

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