Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains

Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 2001.

书目详细资料
主要作者: Aivazian, Dikran A. (Dikran Arvid), 1971-
其他作者: Lawrence J. Stern.
格式: Thesis
语言:eng
出版: Massachusetts Institute of Technology 2005
主题:
在线阅读:http://hdl.handle.net/1721.1/8583
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author Aivazian, Dikran A. (Dikran Arvid), 1971-
author2 Lawrence J. Stern.
author_facet Lawrence J. Stern.
Aivazian, Dikran A. (Dikran Arvid), 1971-
author_sort Aivazian, Dikran A. (Dikran Arvid), 1971-
collection MIT
description Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 2001.
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institution Massachusetts Institute of Technology
language eng
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spelling mit-1721.1/85832019-04-10T09:18:10Z Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains Aivazian, Dikran A. (Dikran Arvid), 1971- Lawrence J. Stern. Massachusetts Institute of Technology. Dept. of Biology. Massachusetts Institute of Technology. Dept. of Biology. Biology. Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 2001. Vita. Includes bibliographical references (leaves 116-131). Protein-lipid interactions are emerging as key components of cellular processes such as protein and membrane trafficking and cell-cell signaling. Many proteins bind lipid reversibly, including cytoplasmic proteins involved in signal transduction, such as Ras and Src. Membrane binding is vital for the function of these signaling proteins both through co-localization with other signaling proteins as well as effects of lipid on intrinsic activities. In this thesis, protein-lipid interactions of subunits of key antigen recognition receptors of the immune system are investigated. The proteins studied are the cytoplasmic domains of immunoreceptor signaling subunits that mediate transmembrane signal transduction in response to receptor engagement. The cytoplasmic domains derive from the T cell receptor, the B cell receptor, Fe receptors and Natural Killer cell stimulatory receptors. The TCR, CD3, CD3, CD3, ... and DAP12 cytoplasmic domains all bind lipid, whereas those of B cell receptor Iga and Igp do not. While all of these proteins are unstructured in solution, ... and CD3 undergo extensive increases in secondary structure upon lipid binding. Lipid binding of ... is found to inhibit its accessibility to kinase-mediated phosphorylation. Based on these results it is proposed that interactions with lipid may regulate the function of receptor cytoplasmic domains, as with many cytosolic proteins involved in signaling processes. by Dikran A. Aivazian. Ph.D. 2005-08-23T21:28:26Z 2005-08-23T21:28:26Z 2001 2001 Thesis http://hdl.handle.net/1721.1/8583 49264584 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 145 leaves 10352221 bytes 10351982 bytes application/pdf application/pdf application/pdf Massachusetts Institute of Technology
spellingShingle Biology.
Aivazian, Dikran A. (Dikran Arvid), 1971-
Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title_full Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title_fullStr Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title_full_unstemmed Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title_short Lipid-protein interactions of immunoreceptor signaling subunit cytoplasmic domains
title_sort lipid protein interactions of immunoreceptor signaling subunit cytoplasmic domains
topic Biology.
url http://hdl.handle.net/1721.1/8583
work_keys_str_mv AT aivaziandikranadikranarvid1971 lipidproteininteractionsofimmunoreceptorsignalingsubunitcytoplasmicdomains