Advances in Immunology, Vol. 109 by Frederick W. Alt (Ed.) PDF

By Frederick W. Alt (Ed.)

ISBN-10: 0123876648

ISBN-13: 9780123876645

Advances in Immunology, a original and hugely revered booklet, offers present advancements in addition to accomplished studies in immunology. Articles handle the big variety of issues that contain immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and medical modalities. Edited and authored via the major scientists within the box, every one quantity offers updated info and instructions for the longer term. * Contributions from major gurus and specialists * Informs and updates on all of the most modern advancements within the box

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Extra info for Advances in Immunology, Vol. 109

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LAT is a TM protein composed of a short (nine-residue) extracellular domain, a TM domain, and an intracellular domain containing several tyrosine residues that are phosphorylated predominantly by ZAP-70 kinase upon TCR ligation and then bind a number of SH2-containing enzymes and adaptor proteins. , 1999a, 2000). Thus, activated LAT serves as an essential scaffold for the assembly of TCR-coupled signaling complexes that mediate productive T cell activation. However, it is not entirely clear how LAT is recruited to the vicinity of the TCR–CD3 complex and TCR-zassociated ZAP-70.

CONCLUDING REMARKS AND PERSPECTIVE The dynamic process of protein palmitoylation (S-acylation) is now well established to play important roles in the function, trafficking, localization, and turnover of many proteins in different cell types. Recent studies have led to substantial progress in our understanding of the mechanisms of protein palmitoylation and, to a lesser extent, protein depalmitoylation. The recent development of sensitive and quantitative methods for the global analysis and profiling of the palmitoyl proteome and the discovery of the diverse DHHC protein family of palmitoylating enzymes open up new avenues of research, and the promise of rapid progress.

129, 2744–2745. Hannoush, R. , and Arenas-Ramirez, N. (2009). Imaging the Lipidome: o-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins. ACS Chem. Biol. 4, 581–587. , and Saito, T. (2010). T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering. Mol. Cell. Biol. 30, 3421–3429. Hawash, I. , Hu, X. , Cassady, J. , Geahlen, R. , and Harrison, M. L. (2002). The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid, inhibits Lck localization to lipid rafts and T cell signaling.

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Advances in Immunology, Vol. 109 by Frederick W. Alt (Ed.)

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