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切換: 標籤 | MARC模式 | ISBD

Analysis and characterization of CAR...

Tanner, Matthew John.

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Analysis and characterization of CARMA1 interacting proteins .

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Analysis and characterization of CARMA1 interacting proteins ./
作者:	Tanner, Matthew John.
面頁冊數:	117 p.
附註:	Adviser: Xin Lin.
Contained By:	Dissertation Abstracts International68-09B.
標題:	Biology, Cell. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3277739
ISBN:	9780549178644

Analysis and characterization of CARMA1 interacting proteins .
Tanner, Matthew John.

Analysis and characterization of CARMA1 interacting proteins . - 117 p.

Adviser: Xin Lin.

Thesis (Ph.D.)--State University of New York at Buffalo, 2007.

The mechanism by which T lymphocytes become activated during an immune response is complex. One important component of T lymphocyte activation is the CARMA1 protein, which plays an essential role in T cell receptor/CD28 costimulation-induced NF-kappaB activation. The CARMA1 protein is composed of a Caspase recruitment domain (CARD), a Coiled-coil domain (CC), as well as a membrane-associated guanylate kinase domain (MAGUK). The objective of this research was to investigate the mechanism by which CARMA1 localizes to the cell membrane, and to uncover novel CARMA1-associated proteins. A series of Yeast Two Hybrid (Y2H) screenings to uncover novel protein-protein interactions were undertaken. A Y2H screen with the N-terminal domains of CARMA1, CARD+CC, revealed an interaction with a truncated CARMA1 protein. Further analysis by co-immunoprecipitation assays demonstrated that CARMA1 can oligomerize through its CC domain, and that oligomerization is independent of cell activation. The relevance of this oligomerization to T cell activation was assessed utilizing oligomerization-deficient CARMA1 mutants, which disrupt physical, functional, and recruitment aspects of CARMA1 signaling. A Y2H screen with the MAGUK domain of CARMA1 revealed a novel binding partner, the Calcium and Integrin Binding protein (CIB1). Physical interaction analysis demonstrates that CIB1 associates with CARMA1 but not with a functionally defective mutant CARMA1 L808P. It was also found that CARMA1 and CIB1 are constitutively associated. While present data suggest a role of the CIB1 protein in TCR signaling, ongoing experimentation is necessary to determine a functional relevance for the CARMA1-CIB1 interaction.

ISBN: 9780549178644Subjects--Topical Terms:

1017686
Biology, Cell.

Analysis and characterization of CARMA1 interacting proteins .
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