Mutation of a gene encoding a protein with extracellular matrix motifs in Usher syndrome type IIa. Eudy, J.D., Weston, M.D., Yao, S., Hoover, D.M., Rehm, H.L., Ma-Edmonds, M., Yan, D., Ahmad, I., Cheng, J.J., Ayuso, C., Cremers, C., Davenport, S., Moller, C., Talmadge, C.B., Beisel, K.W., Tamayo, M., Morton, C.C., Swaroop, A., Kimberling, W.J., Sumegi, J.Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions. Loureiro, J., Ploegh, H.L.Neuroradiology and clinical aspects of Usher syndrome. Tamayo, M.L., Maldonado, C., Plaza, S.L., Alvira, G.M., Tamayo, G.E., Zambrano, M., Frias, J.L., Bernal, J.E.Inhibitory effects of cytomegalovirus proteins US2 and US11 point to contributions from direct priming and cross-priming in induction of vaccinia virus-specific CD8(+) T cells. Basta, S., Chen, W., Bennink, J.R., Yewdell, J.W.Cytomegalovirus US2 destroys two components of the MHC class II pathway, preventing recognition by CD4+ T cells. Tomazin, R., Boname, J., Hegde, N.R., Lewinsohn, D.M., Altschuler, Y., Jones, T.R., Cresswell, P., Nelson, J.A., Riddell, S.R., Johnson, D.C.The usher syndromes. Keats, B.J., Corey, D.P.Usherin, the defective protein in Usher syndrome type IIA, is likely to be a component of interstereocilia ankle links in the inner ear sensory cells. Adato, A., Lefèvre, G., Delprat, B., Michel, V., Michalski, N., Chardenoux, S., Weil, D., El-Amraoui, A., Petit, C.Furthermore, site-directed mutagenesis of the US2 cytoplasmic tail revealed that the most critical residues for class I-induced destruction, cysteine 187, serine 190, tryptophan 193, and phenylalanine 196, occurs every third residue.The lysine-less class I molecules could no longer be dislocated by US2 despite the fact that the interaction between the two proteins was maintained.Although ubiquitin conjugation may occur on the cytosolic tail of the class I MHC molecule, replacement of lysines in the cytosolic tail of heavy chains with arginine does not prevent their degradation by US2.The unique short gene product US2 is a 199-amino acid type I endoplasmic reticulum glycoprotein that modulates surface expression of class I MHC products by targeting class I heavy chains for dislocation from the endoplasmic reticulum to the cytosol, where they undergo proteasomal degradation.We pinpoint these interactions to interactions between the PDZ1 domain of harmonin and the PDZ-binding motifs at the C-termini of the USH2 proteins and NBC3. Īssociations of USH2A with chemical compounds
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