2008 PMBB Symposium Registration Form All fields are required. If the requested information is not applicable to you, type "NA" in that field. If you do not provide a correct e-mail address, your registration cannot be processed, even if you are directed to a confirmation page. Registration information is due by March 20, 2008. NOTICE: It has come to our attention that this form does not function correctly when used with the Apple Safari Web Browser. The form can be used with Internet Explorer and Netscape Navigator. We are sorry for the inconvenience and are working on the situation. . Participant Information Red Fields are Required Information First Name: Last Name: Title: Organization: Address (line 1): Address (line2): City: State: Zip Code : E-mail: Telephone: Fax: Please RSVP by indicating with a YES or NO below what events you will attend: Friday, April 11th, 2008 - Keynote Speaker/Reception - Only Saturday, April 12th, Symposium Event - Only Both Events Will you be submitting an Abstract? Will you be submitting an Abstract Poster? Abstract If you are submitting an abstract, please complete the following: Research Specialization Title of Abstract Please submit your abstract by March 26, 2008. Abstracts should be sent electronically to Ms. Jaynie Holt (Jaynie Holt <holt.96@osu.edu>). They should be submitted as either a MS-Word or an Adobe PDF attachment. On each abstract, please include title, presenter (designated with an asterisk) and their affiliation and e-mail address, and co-authors and their affiliations. Please follow the example format below and limit the abstract to no longer than one page of Times New Roman 12 point type: Submit the abstract following the example below: Example: THE FUNCTION OF F-BOX PROTEIN ATFBL3 IN SUGAR AND ABA SIGNALING IN ARABIDOPSIS THALIANA Wenyan Xiao and Jyan-Chyun Jang Department of Horticulture and Crop Science The Ohio State University, Columbus, OH 43210 GRR1 plays a central role in the glucose signal transduction pathway in the yeast Saccharomyces cerevisiae. Mutations in GRR1 result in a pleiotropic phenotype, including defective glucose signaling, reduced transport of divalent cations and amino acids, and elongated cell morphology. It has been demonstrated recently that GRR1 is an F-box protein, which is a component of E3 ubiquitin protein ligase termed SCF complex, and is required for the degradation of G1 cyclins in cell cycle. To determine whether plant sugar signaling involves a similar component such as yeast GRR1, we have undertaken reverse genetic approaches. On the basis of genomic analyses, we have identified a number of novel Arabidopsis F-box proteins (AtFBL3- AtFBL6) showing high sequence homology to the yeast GRR1. To test whether AtFBLs and the yeast GRR1 are functionally equivalent, we have performed yeast complementation using AtFBL3, with the highest sequence similarity to the yeast GRR1. We have also conducted the same complementation experiment using an Arabidopsis cDNA library. Results showed that none of the Arabidopsis cDNAs could complement the yeast grr1 mutant. To further explore the distinct biological functions of AtFBL3 in Arabidopsis, we have integrated various constructs into transgenic plants that misexpress AtFBL3. Overexpression of AtFBL3 results in reduced sensitivity to the inhibition of seed germination caused by exogenous glucose or ABA. In addition, these transgenic plants are also insensitive to the inhibition of cotyledon expansion and greening, and subsequent shoot development caused by exogenous ABA. Our results indicate that although AtFBL3 can not substitute GRR1 glucose signaling function in yeast, it plays a distinct role in glucose signaling mediated through ABA in plants. Thank You! NOTICE: It has come to our attention that this form does not function correctly when used with the Apple Safari Web Browser. The form can be used with Internet Explorer and Netscape Navigator. We are sorry for the inconvenience and are working on the situation.
All fields are required. If the requested information is not applicable to you, type "NA" in that field. If you do not provide a correct e-mail address, your registration cannot be processed, even if you are directed to a confirmation page.
Registration information is due by March 20, 2008.
NOTICE: It has come to our attention that this form does not function correctly when used with the Apple Safari Web Browser. The form can be used with Internet Explorer and Netscape Navigator. We are sorry for the inconvenience and are working on the situation.
If you are submitting an abstract, please complete the following:
Please submit your abstract by March 26, 2008.
Abstracts should be sent electronically to Ms. Jaynie Holt (Jaynie Holt <holt.96@osu.edu>). They should be submitted as either a MS-Word or an Adobe PDF attachment. On each abstract, please include title, presenter (designated with an asterisk) and their affiliation and e-mail address, and co-authors and their affiliations. Please follow the example format below and limit the abstract to no longer than one page of Times New Roman 12 point type: Submit the abstract following the example below:
Wenyan Xiao and Jyan-Chyun Jang Department of Horticulture and Crop Science The Ohio State University, Columbus, OH 43210 GRR1 plays a central role in the glucose signal transduction pathway in the yeast Saccharomyces cerevisiae. Mutations in GRR1 result in a pleiotropic phenotype, including defective glucose signaling, reduced transport of divalent cations and amino acids, and elongated cell morphology. It has been demonstrated recently that GRR1 is an F-box protein, which is a component of E3 ubiquitin protein ligase termed SCF complex, and is required for the degradation of G1 cyclins in cell cycle. To determine whether plant sugar signaling involves a similar component such as yeast GRR1, we have undertaken reverse genetic approaches. On the basis of genomic analyses, we have identified a number of novel Arabidopsis F-box proteins (AtFBL3- AtFBL6) showing high sequence homology to the yeast GRR1. To test whether AtFBLs and the yeast GRR1 are functionally equivalent, we have performed yeast complementation using AtFBL3, with the highest sequence similarity to the yeast GRR1. We have also conducted the same complementation experiment using an Arabidopsis cDNA library. Results showed that none of the Arabidopsis cDNAs could complement the yeast grr1 mutant. To further explore the distinct biological functions of AtFBL3 in Arabidopsis, we have integrated various constructs into transgenic plants that misexpress AtFBL3. Overexpression of AtFBL3 results in reduced sensitivity to the inhibition of seed germination caused by exogenous glucose or ABA. In addition, these transgenic plants are also insensitive to the inhibition of cotyledon expansion and greening, and subsequent shoot development caused by exogenous ABA. Our results indicate that although AtFBL3 can not substitute GRR1 glucose signaling function in yeast, it plays a distinct role in glucose signaling mediated through ABA in plants.
Wenyan Xiao and Jyan-Chyun Jang
Department of Horticulture and Crop Science
The Ohio State University, Columbus, OH 43210
GRR1 plays a central role in the glucose signal transduction pathway in the yeast Saccharomyces cerevisiae. Mutations in GRR1 result in a pleiotropic phenotype, including defective glucose signaling, reduced transport of divalent cations and amino acids, and elongated cell morphology. It has been demonstrated recently that GRR1 is an F-box protein, which is a component of E3 ubiquitin protein ligase termed SCF complex, and is required for the degradation of G1 cyclins in cell cycle. To determine whether plant sugar signaling involves a similar component such as yeast GRR1, we have undertaken reverse genetic approaches. On the basis of genomic analyses, we have identified a number of novel Arabidopsis F-box proteins (AtFBL3- AtFBL6) showing high sequence homology to the yeast GRR1. To test whether AtFBLs and the yeast GRR1 are functionally equivalent, we have performed yeast complementation using AtFBL3, with the highest sequence similarity to the yeast GRR1. We have also conducted the same complementation experiment using an Arabidopsis cDNA library. Results showed that none of the Arabidopsis cDNAs could complement the yeast grr1 mutant. To further explore the distinct biological functions of AtFBL3 in Arabidopsis, we have integrated various constructs into transgenic plants that misexpress AtFBL3. Overexpression of AtFBL3 results in reduced sensitivity to the inhibition of seed germination caused by exogenous glucose or ABA. In addition, these transgenic plants are also insensitive to the inhibition of cotyledon expansion and greening, and subsequent shoot development caused by exogenous ABA. Our results indicate that although AtFBL3 can not substitute GRR1 glucose signaling function in yeast, it plays a distinct role in glucose signaling mediated through ABA in plants.
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