Por favor, use este identificador para citar o enlazar este ítem: https://hdl.handle.net/10495/39573
Título : Multimolecular signaling complexes enable Syk-mediated signaling of CD36 internalization
Autor : Castaño Monsalve, Diana María
Heit, Bryan
Kim, Hani
Cosio, Gabriela
Collins, Richard
Lowell, Clifford A.
Kain, Kevin C.
Trimble, William S.
Gristein, Sergio
metadata.dc.subject.*: Proteínas Adaptadoras Transductoras de Señales
Adaptor Proteins, Signal Transducing
Western Blotting
Blotting, Western
Antígenos CD36
CD36 Antigens
Metabolismo
Metabolism
Endocitosis
Endocytosis
Inmunoprecipitación
Immunoprecipitation
Péptidos y Proteínas de Señalización Intracelular
Intracellular Signaling Peptides and Proteins
Macrófagos Peritoneales
Macrophages, Peritoneal
Fosforilación
Phosphorylation
Proteínas Tirosina Quinasas
Protein-Tyrosine Kinases
ARN Interferente Pequeño
RNA, Small Interfering
Receptores de IgG
Receptors, IgG
Transducción de Señal
Signal Transduction
Quinasa Syk
Syk Kinase
Tetraspanina 28
Tetraspanin 28
Tetraspanina 29
Tetraspanin 29
https://id.nlm.nih.gov/mesh/D048868
https://id.nlm.nih.gov/mesh/D015153
https://id.nlm.nih.gov/mesh/D018955
https://id.nlm.nih.gov/mesh/D008660
https://id.nlm.nih.gov/mesh/D004705
https://id.nlm.nih.gov/mesh/D047468
https://id.nlm.nih.gov/mesh/D047908
https://id.nlm.nih.gov/mesh/D017737
https://id.nlm.nih.gov/mesh/D010766
https://id.nlm.nih.gov/mesh/D011505
https://id.nlm.nih.gov/mesh/D034741
https://id.nlm.nih.gov/mesh/D017452
https://id.nlm.nih.gov/mesh/D015398
https://id.nlm.nih.gov/mesh/D000072377
https://id.nlm.nih.gov/mesh/D060225
https://id.nlm.nih.gov/mesh/D060245
Fecha de publicación : 2013
Editorial : Cell Press
Elsevier
Citación : Heit B, Kim H, Cosío G, Castaño D, Collins R, Lowell CA, Kain KC, Trimble WS, Grinstein S. Multimolecular signaling complexes enable Syk-mediated signaling of CD36 internalization. Dev Cell. 2013 Feb 25;24(4):372-83. doi: 10.1016/j.devcel.2013.01.007.
Resumen : ABSTRACT: CD36 is a versatile receptor known to play a central role in the development of atherosclerosis, the pathogenesis of malaria, and the removal of apoptotic cells. Remarkably, the short cytosolically exposed regions of CD36 lack identifiable motifs, which has hampered elucidation of its mode of signaling. Using a combination of phosphoprotein isolation, mass spectrometry, superresolution imaging, and gene silencing, we have determined that the receptor induces ligand internalization through a heteromeric complex consisting of CD36, β1 and/or β2 integrins, and the tetraspanins CD9 and/or CD81. This receptor complex serves to link CD36 to the adaptor FcRγ, which bears an immunoreceptor tyrosine activation motif. By coupling to FcRγ, CD36 is able to engage Src-family kinases and Syk, which in turn drives the internalization of CD36 and its bound ligands.
metadata.dc.identifier.eissn: 1878-1551
ISSN : 1534-5807
metadata.dc.identifier.doi: 10.1016/j.devcel.2013.01.007
Aparece en las colecciones: Artículos de Revista en Ciencias Médicas

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