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Canonical and Non-Canonical Plant He...

Miller, Jimi Craig.

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Canonical and Non-Canonical Plant Heterotrimeric G Proteins in Plant Immunity.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Canonical and Non-Canonical Plant Heterotrimeric G Proteins in Plant Immunity./
Author:	Miller, Jimi Craig.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2019,
Description:	133 p.
Notes:	Source: Dissertations Abstracts International, Volume: 81-04, Section: B.
Contained By:	Dissertations Abstracts International81-04B.
Subject:	Plant sciences. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=13809639
ISBN:	9781088320280

Canonical and Non-Canonical Plant Heterotrimeric G Proteins in Plant Immunity.
Miller, Jimi Craig.

Canonical and Non-Canonical Plant Heterotrimeric G Proteins in Plant Immunity. - Ann Arbor : ProQuest Dissertations & Theses, 2019 - 133 p.

Source: Dissertations Abstracts International, Volume: 81-04, Section: B.

Thesis (Ph.D.)--Yale University, 2019.

This item must not be sold to any third party vendors.

Plants contain an innate immune system, which relies on the cell surface receptor FLAGELLIN-SENSITIVE 2 (FLS2) binding to the conserved bacterial molecule flagellin, to initiate immune signaling. The signal from activated FLS2 is transduced by a heterotrimeric G protein complex. This complex consists of a Gα, Gβ, and Gγ subunit and co-localizes with FLS2 at the plasma membrane. It remains unknown whether the heterotrimeric G proteins have additional functions away from signal transduction at the plasma membrane or if additional undiscovered heterotrimeric G subunits exist. Here, I show that two heterotrimeric G protein components function at the endoplasmic reticulum to promote the stability of FLS2. Specifically, the Gβγ heterodimer inhibits the autophagic degradation of FLS2, resulting in stable FLS2 protein levels. In addition to identifying novel functions of the Gβγ heterodimer that promote immune signaling, I also found two potential non-canonical Gβ subunits that negatively regulate immune signaling. I identified two genes, DEFENSE REGULATED WD40-REPEAT 1 and 2 (DRW1 and DRW2), that encode potential non-canonical Gβ subunits. Their predicted protein structure is similar to that of the canonical Gβ subunit ARABIDOPSIS GTP BINDING PROTEIN β-1 SUBUNIT (AGB1). Mutations in both DRW1 and DRW2 results in an increased resistance to both bacterial and fungal pathogen infections, indicating that these potential noncanonical Gβ subunits negatively regulate immune signaling. My studies show first that the heterotrimeric G proteins have novel functions away from the plasma membrane.Second, I have identified new plant heterotrimeric G protein components that are involved in immunity. These results provide insights into how plant heterotrimeric G proteins function independently of their canonical role in signal transduction at the plasma membrane. Additionally, my results provide a foundation for future studies to further elucidate plant immune signaling pathways, and identifies proteins for researchers to manipulate genetically to help bolster immunity against pathogens in crops.

ISBN: 9781088320280Subjects--Topical Terms:

3173832
Plant sciences.

Canonical and Non-Canonical Plant Heterotrimeric G Proteins in Plant Immunity.
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300 $a 133 p.
500 $a Source: Dissertations Abstracts International, Volume: 81-04, Section: B.
500 $a Advisor: Clay, Nicole K.
502 $a Thesis (Ph.D.)--Yale University, 2019.
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506 $a This item must not be added to any third party search indexes.
520 $a Plants contain an innate immune system, which relies on the cell surface receptor FLAGELLIN-SENSITIVE 2 (FLS2) binding to the conserved bacterial molecule flagellin, to initiate immune signaling. The signal from activated FLS2 is transduced by a heterotrimeric G protein complex. This complex consists of a Gα, Gβ, and Gγ subunit and co-localizes with FLS2 at the plasma membrane. It remains unknown whether the heterotrimeric G proteins have additional functions away from signal transduction at the plasma membrane or if additional undiscovered heterotrimeric G subunits exist. Here, I show that two heterotrimeric G protein components function at the endoplasmic reticulum to promote the stability of FLS2. Specifically, the Gβγ heterodimer inhibits the autophagic degradation of FLS2, resulting in stable FLS2 protein levels. In addition to identifying novel functions of the Gβγ heterodimer that promote immune signaling, I also found two potential non-canonical Gβ subunits that negatively regulate immune signaling. I identified two genes, DEFENSE REGULATED WD40-REPEAT 1 and 2 (DRW1 and DRW2), that encode potential non-canonical Gβ subunits. Their predicted protein structure is similar to that of the canonical Gβ subunit ARABIDOPSIS GTP BINDING PROTEIN β-1 SUBUNIT (AGB1). Mutations in both DRW1 and DRW2 results in an increased resistance to both bacterial and fungal pathogen infections, indicating that these potential noncanonical Gβ subunits negatively regulate immune signaling. My studies show first that the heterotrimeric G proteins have novel functions away from the plasma membrane.Second, I have identified new plant heterotrimeric G protein components that are involved in immunity. These results provide insights into how plant heterotrimeric G proteins function independently of their canonical role in signal transduction at the plasma membrane. Additionally, my results provide a foundation for future studies to further elucidate plant immune signaling pathways, and identifies proteins for researchers to manipulate genetically to help bolster immunity against pathogens in crops.
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