Signalling versatility following self and non-self sensing by myeloid C-type lectin receptors
Among myeloid immune receptors, C-type lectin receptors (CLRs) have a remarkable capacity to sense a variety of self and non-self ligands. The coupling of CLRs to different signal transduction modules is influenced not only by the receptor, but also by the nature, density and architecture of the lig...
| Autores: | , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2015 |
| País: | España |
| Institución: | Instituto de Salud Carlos III (ISCIII) |
| Repositorio: | Repisalud |
| Idioma: | inglés |
| OAI Identifier: | oai:repisalud.isciii.es:20.500.12105/5520 |
| Acceso en línea: | http://hdl.handle.net/20.500.12105/5520 |
| Access Level: | acceso abierto |
| Palabra clave: | Innate immunity C-type lectin receptors Myeloid cells PATTERN-RECOGNITION RECEPTOR DENDRITIC CELL-RECEPTOR INDUCED NEUTROPHIL ACTIVATION SYK TYROSINE KINASE DC-SIGN FCR-GAMMA INFLAMMATORY RESPONSES CANDIDA-ALBICANS IMMUNE-RESPONSES DECTIN-2 RECOGNITION |
| Sumario: | Among myeloid immune receptors, C-type lectin receptors (CLRs) have a remarkable capacity to sense a variety of self and non-self ligands. The coupling of CLRs to different signal transduction modules is influenced not only by the receptor, but also by the nature, density and architecture of the ligand, which can affect the rate of receptor internalization and trafficking to diverse intracellular compartments. Understanding how the variety of self and non-self ligands triggers differential CLR signalling and function presents a fascinating biological challenge. Non-self ligands usually promote inflammation and immunity, whereas self ligands are frequently involved in communication and tolerance. But pathogens can mimic self-inhibitory signals to escape immune surveillance, and endogenous ligands can contribute to the sensing of pathogens through CLRs. In this review, we survey the complexity and flexibility in functional outcome found in the myeloid CLRs, which is not only based on their differing intracellular motifs, but is also conditioned by the physical nature, affinity and avidity of the ligand. (C) 2014 The Authors. Published by Elsevier GmbH. |
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