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008			220708b xxu||||| |||| 00| 0 eng d
040			_cH12O
041			_aeng
100			_93076 _aRoda Navarro, Pedro _eInstituto de Investigación imas12
245	0	0	_aDistinct Trafficking of Cell Surface and Endosomal TIM-1 to the Immune Synapse. _h[artículo]
260			_bTraffic (Copenhagen, Denmark), _c2015
300			_a16(11):1193-207.
500			_aFormato Vancouver: Echbarthi M, Zonca M, Mellwig R, Schwab Y, Kaplan G, DeKruyff RH et al. Distinct Trafficking of Cell Surface and Endosomal TIM-1 to the Immune Synapse. Traffic. 2015 Nov;16(11):1193-207.
501			_aPMID: 26332704 PMC4607657
504			_aContiene 42 referencias
520			_aThe 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.
710			_9625 _aInstituto de Investigación imas12
856			_uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4607657/ _yAcceso libre
942			_2ddc _cART _n0