Title

Role of Zebrafish GADD34 in Regulating Protein Synthesis in Response to ER Stress

Poster Number

49

Lead Author Major

Pre-Dentistry and Biological Sciences

Format

Poster Presentation

Faculty Mentor Name

Doug Weiser

Faculty Mentor Department

Biological Sciences

Abstract/Artist Statement

Eukaryotic cells respond to accumulation of unfolded proteins in the endoplasmic reticulum (ER) by phosphorylating the alpha subunit of eukaryotic translation initiation factor 2 (eIF- 2alpha), inhibiting translation. ER stress is compensated by kinase activity, terminating general protein synthesis, however, few transcripts are activated, thereupon activating other downstream genes such as growth arrest and DNA damage-inducible protein 34 (GADD34), triggering a negative feedback response to the attenuation of protein synthesis. Studies of GADD34 have shown GADD34 to interact with protein phosphatase 1 (PP1), resulting in the dephosphorylation of eIF-2alpha, allowing translation of proteins to ensue once more. The strength of this GADD34 negative feedback mechanism determines whether ER stress induced cells will initiate apoptosis, or overcome the stress response and survive. In this particular study, Zebrafish embryos and GADD34 transcripts were used to further comprehend the expression and mode of action of GADD34 in ER stress induced cells. The rapid uptake of ER stress-inducing drug, Thapsigargin, and the ease of distinct visualization of the expressed gene made Zebrafish embryos a favorable organism of study. In situ hybridization of dechorinated Zebrafish embryos using sense and anti-sense RNA GADD34 probes were attempted to visualize the expression of GADD34 in stress-induced embryos. Various transcripts with deletion mutations were generated using PCR, and observed in cancer cells to determine different domain interactions with PP1 and subcellular localization of GADD34. By observing the expression patterns of GADD34 in Zebrafish embryos and cancer cells, we hope to obtain greater understanding of protein regulation within mammalian cells.

Location

DeRosa University Center, Ballroom

Start Date

20-4-2013 1:00 PM

End Date

20-4-2013 3:00 PM

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Apr 20th, 1:00 PM Apr 20th, 3:00 PM

Role of Zebrafish GADD34 in Regulating Protein Synthesis in Response to ER Stress

DeRosa University Center, Ballroom

Eukaryotic cells respond to accumulation of unfolded proteins in the endoplasmic reticulum (ER) by phosphorylating the alpha subunit of eukaryotic translation initiation factor 2 (eIF- 2alpha), inhibiting translation. ER stress is compensated by kinase activity, terminating general protein synthesis, however, few transcripts are activated, thereupon activating other downstream genes such as growth arrest and DNA damage-inducible protein 34 (GADD34), triggering a negative feedback response to the attenuation of protein synthesis. Studies of GADD34 have shown GADD34 to interact with protein phosphatase 1 (PP1), resulting in the dephosphorylation of eIF-2alpha, allowing translation of proteins to ensue once more. The strength of this GADD34 negative feedback mechanism determines whether ER stress induced cells will initiate apoptosis, or overcome the stress response and survive. In this particular study, Zebrafish embryos and GADD34 transcripts were used to further comprehend the expression and mode of action of GADD34 in ER stress induced cells. The rapid uptake of ER stress-inducing drug, Thapsigargin, and the ease of distinct visualization of the expressed gene made Zebrafish embryos a favorable organism of study. In situ hybridization of dechorinated Zebrafish embryos using sense and anti-sense RNA GADD34 probes were attempted to visualize the expression of GADD34 in stress-induced embryos. Various transcripts with deletion mutations were generated using PCR, and observed in cancer cells to determine different domain interactions with PP1 and subcellular localization of GADD34. By observing the expression patterns of GADD34 in Zebrafish embryos and cancer cells, we hope to obtain greater understanding of protein regulation within mammalian cells.