Distinct but Dispensable N-Glycosylation of Human CD69 Proteins
作者： Barbara A. Vance , Michael J. Bennett , Yvona Ward , Ronald G. Gress , Kelly P. Kearse
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摘要: Human CD69 is uniquely glycosylated at typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) motifs, which represents the molecular basis for formation of homodimers heterodimers. Here we examined importance N-glycosylation assembly intracellular transport proteins using mutant molecules that specifically lack N-glycan attachment motifs. These studies verify Cys residues in triplet sequences addition to human endoplasmic reticulum (ER). In addition, these data demonstrate monoglycosylated (bearing N-glycans exclusively or sites) aglycosylated (lacking N-glycans) efficiently dimerize ER have similar stability as wild-type molecules. Finally, results show lacking sites are transported plasma membrane.
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sci-hub.se 参考文章(16)
B. Holst, A. W. Bruun, M. C. Kielland-Brandt, J. R. Winther, Competition between folding and glycosylation in the endoplasmic reticulum. The EMBO Journal. ,vol. 15, pp. 3538- 3546 ,(1996) , 10.1002/J.1460-2075.1996.TB00723.X
K.P. Kearse, J.L. Roberts, T.I. Munitz, D.L. Wiest, T. Nakayama, A. Singer, Developmental regulation of alpha beta T cell antigen receptor expression results from differential stability of nascent TCR alpha proteins within the endoplasmic reticulum of immature and mature T cells. The EMBO Journal. ,vol. 13, pp. 4504- 4514 ,(1994) , 10.1002/J.1460-2075.1994.TB06772.X
J Bajorath, A Aruffo, Molecular model of the extracellular lectin-like domain in CD69. Journal of Biological Chemistry. ,vol. 269, pp. 32457- 32463 ,(1994) , 10.1016/S0021-9258(18)31657-0
H Fiebig, J Hamann, M Strauss, Expression Cloning of the Early Activation Antigen CD69, a Type II Integral Membrane Protein With a C-type Lectin Domain Journal of Immunology. ,vol. 150, pp. 4920- 4927 ,(1993)
J P Miletich, G J Broze, Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. Journal of Biological Chemistry. ,vol. 265, pp. 11397- 11404 ,(1990) , 10.1016/S0021-9258(19)38606-5
E. M. Shevach, J. E. Coligan, G. Stingl, G. M. B. Pereira, P. J. Kehn, F. Koning, W. M. Yokoyama, Characterization of a cell surface-expressed disulfide-linked dimer involved in murine T cell activation. Journal of Immunology. ,vol. 141, pp. 369- 376 ,(1988)
E Bause, G Legler, The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis Biochemical Journal. ,vol. 195, pp. 639- 644 ,(1981) , 10.1042/BJ1950639
Barbara A. Vance, Wenyu Wu, Randall K. Ribaudo, David M. Segal, Kelly P. Kearse, Multiple Dimeric Forms of Human CD69 Result from Differential Addition of N-Glycans to Typical (Asn-X-Ser/Thr) and Atypical (Asn-X-Cys) Glycosylation Motifs Journal of Biological Chemistry. ,vol. 272, pp. 23117- 23122 ,(1997) , 10.1074/JBC.272.37.23117
L L Lanier, D W Buck, L Rhodes, A Ding, E Evans, C Barney, J H Phillips, INTERLEUKIN 2 ACTIVATION OF NATURAL KILLER CELLS RAPIDLY INDUCES THE EXPRESSION AND PHOSPHORYLATION OF THE Leu-23 ACTIVATION ANTIGEN Journal of Experimental Medicine. ,vol. 167, pp. 1572- 1585 ,(1988) , 10.1084/JEM.167.5.1572
Ana G. Santis, Manuel López-Cabrera, Jörg Hamann, Michael Strauss, Francisco Ánchez-Madrid, Structure of the gene coding for the human early lymphocyte activation antigen CD69: a C-type lectin receptor evolutionarily related with the gene families of natural killer cell-specific receptors. European Journal of Immunology. ,vol. 24, pp. 1692- 1697 ,(1994) , 10.1002/EJI.1830240735