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Intracellular trafficking of TIM-1 towards cell-cell contacts in the context of lymphocyte activation
Author
Echbarthi, MeriemAdvisor
Casanovas Suelves, José MaríaEntity
UAM. Departamento de Biología Molecular; CSIC. Centro Nacional de Biotecnología (CNB)Date
2015-03-16Subjects
Linfocitos - Tesis doctorales; Proteínas de la membrana - Tesis doctorales; Biología y Biomedicina / BiologíaNote
Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departamento de Biología Molecular. Fecha de lectura: 16-03-2015Esta obra está bajo una licencia de Creative Commons Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional.
Abstract
T cell/Transmembrane Immunoglobulin and Mucin domain protein-1
(TIM-1) has been linked to asthma, allergy and atopic diseases. TIM-1
preferentially locates in intracellular compartments. Our results have
demonstrated that both human and mouse TIM-1 locate in different types of
endosomes and TIM-1 structural domains are important for TIM-1 sorting in
intracellular vesicles. BALB/c variant of mouse TIM-1 has a longer mucin
domain and it is more efficiently sorted to intracellular vesicle than C57BL/6
variant with shorter mucin domain. High-affinity ligands of TIM-1 such as PtdSer
increase the amount of TIM-1 at cell surface. TIM-1 accumulates at intercellular
junctions of transfected cells (homotypic TIM1-TIM1 interaction) and cellular
contacts with apoptotic cells and it could be transferred through exosomes to
recipient (apoptotic) cells. TIM-1 accumulation at cell-cell contacts is N-terminal
domain and MILIBS dependent. This interaction could be mediated by PtdSer
or by an undetermined co-factor that induces direct interaction between
molecules of opposite cells.
It has been reported that TIM-1 is physically associated with CD3, a
major component of T cell receptor (TCR). Our results show that major
intracellular pool of TIM-1 translocates to immunological synapse (IS) and
colocalizes with CD3 in central supramolecular activating cluster (cSMAC),
where it can enhance antigen-dependent T cell response in association with
CD3-TCR. Nevertheless, cell surface TIM-1 does not translocate to IS and
locates away from it. Hence, cellular localization of TIM-1 determines its
differential trafficking in T cells during IS formation. Actually, increase of cell
surface TIM-1 by interaction with liposomes exposing PtdSer prevents its
translocation to IS. This could explain why TIM-1 has
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