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Virginia Tech

1. Li, Jianhui. Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development.

Degree: PhD, Plant Pathology, Physiology, and Weed Science, 2017, Virginia Tech

Cornichon (CNI) proteins are a conserved family of proteins among eukaryotes, from Erv14 in the yeast Saccharomyces cerevisiae to CNI homologs (CNIHs) in mammals and plants. Erv14 functions as a cargo receptor of coat protein complex II (COPII) for protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus, en route to their final destinations. By interacting with specific cargo proteins, CNI proteins regulate key steps of embryo polarity in Drosophila, budding in yeast, and synaptic transmission in the mammalian brain. However, we have very limited understanding of plant CNIHs. Positive-strand RNA viruses assemble their viral replication complexes (VRCs) at specific host organelle membranes. With a better understanding of host factors involved in targeting viral replication proteins to the preferred organelles, we expect to block trafficking of viral replication proteins and thus, viral infection, by manipulating the required host proteins. Brome mosaic virus (BMV) is a model of positive-strand RNA viruses and its replication can be recapitulated in yeast. Importantly, BMV replication protein 1a is the only required viral protein to form VRCs at the perinuclear ER membrane in yeast. I demonstrate that Erv14 and COPII coat proteins are required for targeting BMV 1a to the perinuclear ER in yeast, suggesting a novel function of COPII vesicles in protein trafficking to the perinuclear ER membrane and in the BMV VRC formation. As for cellular functions, I show that plant CNIHs complement the defective distribution of BMV 1a in yeast mutant lacking Erv14. Taking advantage of Arabidopsis thaliana knockout mutants and knockdown of gene expression in Nicotiana benthamina, I also discover that CNIHs unexpectedly play crucial roles in pollen development, infection of a bacterial pathogen, and maintenance of ER tubules. I further confirm that CNI proteins are also required for maintaining ER tubules in yeast, suggesting a novel and conserved role in shaping ER morphology. Therefore, these findings indicate the functional diversity and redundancy of CNI proteins in key cellular processes and suggest a novel strategy to control plant pathogenic viruses and bacteria by manipulating plant CNIHs. Advisors/Committee Members: Wang, Xiaofeng (committeechair), Vinatzer, Boris A. (committee member), McDowell, John M. (committee member), Meng, Xiang-Jin (committee member).

Subjects/Keywords: positive-strand RNA virus; cornichon proteins; protein trafficking; early secretory pathway; ER morphology; pollen development; bacterial infection

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Li, J. (2017). Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development. (Doctoral Dissertation). Virginia Tech. Retrieved from http://hdl.handle.net/10919/77687

Chicago Manual of Style (16th Edition):

Li, Jianhui. “Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development.” 2017. Doctoral Dissertation, Virginia Tech. Accessed November 22, 2019. http://hdl.handle.net/10919/77687.

MLA Handbook (7th Edition):

Li, Jianhui. “Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development.” 2017. Web. 22 Nov 2019.

Vancouver:

Li J. Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development. [Internet] [Doctoral dissertation]. Virginia Tech; 2017. [cited 2019 Nov 22]. Available from: http://hdl.handle.net/10919/77687.

Council of Science Editors:

Li J. Cornichon Proteins: Unexpected Roles in Plant Pathogen Infection, ER Morphology Maintenance and Pollen Development. [Doctoral Dissertation]. Virginia Tech; 2017. Available from: http://hdl.handle.net/10919/77687

2. Das, Vaijayanti. STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC.

Degree: MSin Biology, College of Sciences and Health Professions, 2012, Cleveland State University

Proteins destined for secretion, after folding and the initial modification in the endoplasmic reticulum (ER), are transported to the ERGIC and then to Golgi stacks, before being sorted into their final destinations. Collectively these proteins that move through the secretory pathway are known as cargo proteins. Some of the soluble cargo proteins require cargo receptors to be efficiently packaged into vesicles exiting the ER. Evidence for the presence of such receptors in mammals came from the studies of a genetic disorder called the combined deficiency of factor V (FV) and factor VIII (FVIII) or F5F8D. F5F8D patients have mutations in either of the two genes - LMAN1 or MCFD2. LMAN1 and MCFD2 form a receptor complex that facilitates the ER to Golgi transport of FV and FVIII. Distinct binding sites for FV and FVIII exist on LMAN1 and MCFD2, but the specific location of these binding sites are not known. Ambiguity exists on the mechanism of cargo release by LMAN1 and MCFD2. Like FV and FVIII, other LMAN1 cargos (cathepsin C, Z and a-1 antitrypsin) are also glycosylated. Thus the sugar binding activity of carbohydrate recognition domain (CRD) of LMAN1 is presumably important for the recognition of the cargo glycoprotein. Using biochemical approaches we determined the locations of sugar binding sites and their importance in cargo binding. We successfully purified the CRD of LMAN1 using a denaturation/refolding protocol. Using isothermal titration calorimetry (ITC) assay, we confirmed that our purified CRD is a functional protein by its ability to bind to 2 calcium ions. ITC assay also provided insight on the effect of pH on binding ability of CRD to calcium as well as revealed the binding affinity of CRD towards its ligand a1-2 mannobiose. In collaboration with Dr. Saurav Misra's lab, we solved the structure of mannobiose bound CRD which revealed key amino acids involved in ligand binding. Mutations of these amino acids in LMAN1 were constructed to reconfirm their importance in sugar binding in vivo. These biochemical studies will provide a useful insight into the mechanism of cargo binding in the ER and release in the ERGIC and Golgi. Advisors/Committee Members: Zhang, Bin (Advisor).

Subjects/Keywords: Biochemistry; Mechanism of protein trafficking in the early secretory pathway

…CHAPTER I INTRODUCTION 1.1 The early secretory pathway Up to one third of cellular proteins… …early secretory pathway (Figure 1) refers to the transport of proteins from the ER… …in . 13 mammalian cells. The early secretory pathway is highlighted by the purple box… …Traffic through the early secretory pathway is same for all newly synthesized proteins enroute… …They undergo trimming and processing at the early secretory pathway in order to be… 

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APA (6th Edition):

Das, V. (2012). STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC. (Masters Thesis). Cleveland State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=csu1343398252

Chicago Manual of Style (16th Edition):

Das, Vaijayanti. “STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC.” 2012. Masters Thesis, Cleveland State University. Accessed November 22, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=csu1343398252.

MLA Handbook (7th Edition):

Das, Vaijayanti. “STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC.” 2012. Web. 22 Nov 2019.

Vancouver:

Das V. STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC. [Internet] [Masters thesis]. Cleveland State University; 2012. [cited 2019 Nov 22]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=csu1343398252.

Council of Science Editors:

Das V. STRUCTURAL BASIS OF LMAN1 CARGO CAPTURE IN ER & RELEASE IN ERGIC. [Masters Thesis]. Cleveland State University; 2012. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=csu1343398252

3. Marais, Claire-Line. Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana.

Degree: Docteur es, Sciences, technologie, santé. Biologie végétale, 2013, Université de Bordeaux Segalen

Les protéines SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) sont essentielles pour la fusion membranaire. J'ai étudié chez Arabidopsis thaliana la SNARE Memb11 de l’appareil de Golgi qui intervient au début de la voie sécrétoire à l'interface Réticulum endoplasmique (RE)-appareil de Golgi. Dans les cellules de mammifères, l'orthologue de Memb11 (Membrine) est un « récepteur » potentiel de la GTPase Arf1 à la membrane golgienne. Cette dernière est impliquée dans le recrutement de la machinerie COPI nécessaire au transport rétrograde de l'appareil de Golgi vers le RE. Le but de ce travail était de déterminer si Memb11 pouvait interagir avec Arf1 dans les cellules végétales. Des anticorps dirigés contre la partie cytosolique de Memb11 ont été obtenus et ont été utilisés sur tissus végétaux pour réaliser des immunomarquages en microscopie électronique à transmission et des immunoprécipitations sur extraits de plantes. Il a été démontré que Memb11 est située au niveau de la membrane cis-golgienne et qu'elle co-immunoprécipite avec Arf1, suggérant ainsi que Arf1 peut interagir avec Memb11. J'ai confirmé l'interaction de Memb11 et Arf1 au niveau de l'appareil de Golgi par des expériences de BiFC (Bimolecular Fluorescence Complementation) in vivo. Cette interaction est spécifique puisque ni Memb12 (90% d'identité avec Memb11) ni Sec22 interagissent avec Arf1. Grâce à une approche de bioinformatique structurale, j'ai déterminé les régions de Memb11 (différentes de Memb12) qui pourraient être critiques pour l'interaction et j’ai commencé à tester in vivo les mutants correspondants par BiFC. En outre, des expériences d’immunoprécipitations avec des protéines recombinantes produites in vitro suggèrent que la forme d’Arf1 liée au GTP interagit avec Memb11.

The SNARE proteins (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) are critical for membrane fusion in the secretory pathway. I have studied the Golgi SNARE Memb11 in Arabidopsis thaliana cells. Memb11 is involved at the ER-Golgi interface. In mammalian cells, the ortholog of Memb11 (Membrin) is the potential “receptor” of the GTPase Arf1 in the Golgi membrane. This protein is involved for the recruitment of the COPI machinery, required for retrograde transport from the Golgi to the ER. The aim of this work was to determine whether Memb11 can interact with Arf1 in plant cells. Antibodies against the cytosolic part of Memb11 were obtained and were applied on plant tissues to perform immunolabeling by transmission electron microscopy and immunoprecipitation (IP) studies. It has been shown that Memb11 is located at the cis-Golgi and that it co-immunoprecipated with Arf1, suggesting that Arf1 may interact with Memb11. I confirmed the interaction of Memb11 and Arf1 at the Golgi by in vivo BiFC (Bimolecular Fluorescence Complementation) experiments. This interaction was specific since neither Memb12 (90% identity with Memb11) nor Sec22 interacted with ARF1. Thanks to a structural bioinformatic approach, I determined the…

Advisors/Committee Members: Moreau, Patrick (thesis director).

Subjects/Keywords: SNARE; Memb11; GTPase; ARF1; Voie sécrétoire; Appareil de Golgi; Reticulum endoplasmique; SNARE; Memb11; GTPase; Arf1; Early secretory pathway; Golgi apparatus; Endoplasmic Reticulum

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Marais, C. (2013). Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana. (Doctoral Dissertation). Université de Bordeaux Segalen. Retrieved from http://www.theses.fr/2013BOR22105

Chicago Manual of Style (16th Edition):

Marais, Claire-Line. “Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana.” 2013. Doctoral Dissertation, Université de Bordeaux Segalen. Accessed November 22, 2019. http://www.theses.fr/2013BOR22105.

MLA Handbook (7th Edition):

Marais, Claire-Line. “Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana.” 2013. Web. 22 Nov 2019.

Vancouver:

Marais C. Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana. [Internet] [Doctoral dissertation]. Université de Bordeaux Segalen; 2013. [cited 2019 Nov 22]. Available from: http://www.theses.fr/2013BOR22105.

Council of Science Editors:

Marais C. Rôle de la SNARE Memb11 comme « récepteur » de la GTPase Arf1 à l’appareil de Golgi chez Arabidopsis thaliana : Role of the SNARE Memb11 as "receptor" of the GTPase Arf1 at the Golgi apparatus of Arabidopsis thaliana. [Doctoral Dissertation]. Université de Bordeaux Segalen; 2013. Available from: http://www.theses.fr/2013BOR22105

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