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An amino-terminal region of Caenorha...

Patikoglou, Georgia Anastasia.

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An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling.

Record Type:	Electronic resources : Monograph/item
Title/Author:	An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling./
Author:	Patikoglou, Georgia Anastasia.
Description:	338 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1232.
Contained By:	Dissertation Abstracts International64-03B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084350
ISBN:	0496321579

An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling.
Patikoglou, Georgia Anastasia.

An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling. - 338 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1232.

Thesis (Ph.D.)--Yale University, 2003.

Regulators of G protein signaling (RGS proteins) contain an RGS domain that inhibits Galpha signaling by activating Galpha GTPase activity. Certain RGS proteins also contain a G gamma-like (GGL) domain and a poorly-characterized but conserved N-terminal region. We assessed the functions of these subregions in the C. elegans RGS proteins EGL-10 and EAT-16, which selectively inhibit GOA-1 (Galphao) and EGL-30 (Galphaq), respectively.

ISBN: 0496321579Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling.
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100 1 $a Patikoglou, Georgia Anastasia. $3 1931888
245 1 3 $a An amino-terminal region of Caenorhabditis elegans RGS proteins EGL-10 and EAT-16 directs inhibition of heterotrimeric G protein signaling.
300 $a 338 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1232.
500 $a Director: Michael R. Koelle.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 $a Regulators of G protein signaling (RGS proteins) contain an RGS domain that inhibits Galpha signaling by activating Galpha GTPase activity. Certain RGS proteins also contain a G gamma-like (GGL) domain and a poorly-characterized but conserved N-terminal region. We assessed the functions of these subregions in the C. elegans RGS proteins EGL-10 and EAT-16, which selectively inhibit GOA-1 (Galphao) and EGL-30 (Galphaq), respectively.
520 $a We determined that the GGL domain in EGL-10 and EAT-16 mediates binding to a unique, divergent Gbeta isoform homologous to Gbeta5 in mammals, known as GPB-2 in C. elegans. Using Western analysis, we assessed the levels of GPB-2 and RGS proteins in animals mutant for these proteins. We found that these proteins depend on each other for expression and/or stability. In addition, immunoprecipitation experiments showed that GPB-2 does indeed associate with EAT-16 and EGL-10.
520 $a To assess the role of the conserved N-terminal region, we used transgenes in C. elegans to express EGL-10, EAT-16, their subregions, or EGL-10/EAT-16 chimeras in animals mutant for these RGS proteins. The chimeras showed that the GGURGS region of either protein can act on either GOA-1 or EGL-30 and that a key factor determining Ga target selectivity is the manner in which the N-terminal and GGURGS regions are linked. We also found that coexpressing N-terminal and GGURGS fragments of EGL-10 gave full EGL-10 activity, while either fragment alone gave little activity. Biochemical analysis showed that coexpressing the two fragments caused both to increase in abundance and also caused the GGURGS fragment to move to the membrane, where the N-terminal fragment is localized. By coimmunoprecipitation we found that the N-terminal fragment complexes with the C-terminal fragment and its associated Gbeta subunit, GPB-2. We conclude that the N-terminal region directs inhibition of Galpha signaling by forming a complex with the GGURGS region and affecting its stability, membrane localization and Galpha target specificity.
590 $a School code: 0265.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
650 4 $a Biology, Neuroscience. $3 1017680
690 $a 0487
690 $a 0786
690 $a 0317
710 2 0 $a Yale University. $3 515640
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Koelle, Michael R., $e advisor
790 $a 0265
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084350