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Proteomic Analysis of SUMO Mediated Stress Responses in Yeast
Author(s) -
Ro Kevin,
Wohlschlegel James
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.605.1
Subject(s) - dna damage , sumo protein , microbiology and biotechnology , biology , proteomics , cellular stress response , ubiquitin , computational biology , nocodazole , genome instability , fight or flight response , cell , genetics , dna , gene , cytoskeleton
Cells are constantly exposed to a wide variety of environmental stresses and their ability to maintain the integrity of their genome is essential to their survival. One cellular pathway that plays a key role in this cellular response is the SUMO modification pathway. SUMO is a member of the ubiquitin family of small protein modifiers and its covalent attachment to cellular targets is a critical regulatory step for a diverse range of cellular processes that includes transcriptional regulation, cell cycle progression, and cellular DNA damage response. In this study we are investigating how patterns of targets modified by SUMO changes in response to various stresses such as hydrogen peroxide, ethanol, nocodazole, and doxorubicin. This approach involves the use of a quantitative proteomics platform established in our laboratory and is built around a recently developed linear ion trap–orbitrap hybrid mass spectrometer. Ultimately, this work will enable us to understand how cells use SUMO pathways to protect themselves from genotoxic damage and offer insight into how the deregulation of this pathway, a common feature in cancers, may lead to genetic instability. These experiments are currently underway and the results from this work will be presented. Importantly, the SUMO pathway is highly conserved between yeast and humans so that important findings generated by our analysis will likely be directly applicable to humans.