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Analysis and characterization of CAR...

Tanner, Matthew John.

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Analysis and characterization of CARMA1 interacting proteins .

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Analysis and characterization of CARMA1 interacting proteins ./
Author:	Tanner, Matthew John.
Description:	117 p.
Notes:	Adviser: Xin Lin.
Contained By:	Dissertation Abstracts International68-09B.
Subject:	Biology, Cell. -
Online resource:	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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020 $a 9780549178644
035 $a (UMI)AAI3277739
035 $a AAI3277739
040 $a UMI $c UMI
100 1 $a Tanner, Matthew John. $3 1269357
245 1 0 $a Analysis and characterization of CARMA1 interacting proteins .
300 $a 117 p.
500 $a Adviser: Xin Lin.
500 $a Source: Dissertation Abstracts International, Volume: 68-09, Section: B, page: 5728.
502 $a Thesis (Ph.D.)--State University of New York at Buffalo, 2007.
520 $a 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.
590 $a School code: 0656.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0379
690 $a 0410
710 2 $a State University of New York at Buffalo. $b Microbiology and Immunology. $3 1025245
773 0 $t Dissertation Abstracts International $g 68-09B.
790 $a 0656
790 1 0 $a Lin, Xin, $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3277739