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Localization of the protein tyrosine...

Fawcett, Vicki Collins Johnson.

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Localization of the protein tyrosine phosphatase SHP-1 to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl-terminus.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Localization of the protein tyrosine phosphatase SHP-1 to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl-terminus./
作者:	Fawcett, Vicki Collins Johnson.
面頁冊數:	124 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0186.
Contained By:	Dissertation Abstracts International66-01B.
標題:	Health Sciences, Immunology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3161230
ISBN:	9780496948147

Localization of the protein tyrosine phosphatase SHP-1 to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl-terminus.
Fawcett, Vicki Collins Johnson.

Localization of the protein tyrosine phosphatase SHP-1 to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl-terminus. - 124 p.

Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0186.

Thesis (Ph.D.)--University of Virginia, 2005.

The protein tyrosine phosphatase SHP-1 has been shown to be a negative regulator of signaling mediated via the T cell receptor (TCR). A growing body of evidence indicates that the regulated localization of proteins within certain membrane subdomains, commonly referred to as lipid rafts, is important for the successful transduction of signaling events downstream of the TCR/CD3 complex. However, considerably less is known about the localization of negative regulators during these lipid rafts-dependent signaling events. Here, we have investigated the subcellular localization of SHP-1 and its role in the regulation of TCR-mediated signaling. Our studies demonstrate that, in a murine T cell hybridoma as well as in primary murine thymocytes, approximately 20--30% of total cellular SHP-1 localizes to the lipid rafts, both basally and following TCR stimulation. Interestingly, while SHP-1 isolated from the detergent-soluble fractions is tyrosyl phosphorylated, SHP-1 isolated from the lipid rafts lacks the TCR-induced tyrosine phosphorylation, suggesting Physical and/or functional differences between these two subpopulations. Additionally, mutational analyses identify a requirement for the carboxyl-terminal residues of SHP-1 in optimal localization to lipid rafts. While expression of SHP-1 that localizes to lipid rafts potently inhibits TCR-mediated early signaling events and IL-2 production, lipid-rafts-excluded SHP-1 mutants fail to elicit any of the inhibitory effects. Taken together, these studies indicate that the carboxyl-terminus of SHP-1 is at least partially responsible for localization to the lipid rafts, possibly owing to a post-translational modification, and reveal a key role for lipid rafts localization of SHP-1 in mediating the inhibitory effects on TCR-mediated signaling events.

ISBN: 9780496948147Subjects--Topical Terms:

1017716
Health Sciences, Immunology.

Localization of the protein tyrosine phosphatase SHP-1 to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl-terminus.
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