FCH/CIP4 homology-Bin-Amphiphysin-Rvs (F-BAR) domain proteins are a subfamily of the Bin-Amphiphysin-Rvs (BAR) superfamily of proteins. They contain unique domains that bind and reshape the phospholipid bilayers of endosomal compartments during endocytosis. Using a functional assay for cell survival, we identified an F-BAR protein, FCH/CIP4 homology and double Src homology 3 domains 2 (FCHSD2), that confers drug resistance. Stable expression of shRNA against FCHSD2 in multiple cell types showed that loss of FCHSD2 sensitized cells to apoptosis by doxorubicin. Silencing of FCHSD2 also enhanced the ability of fibroblasts to grow colonies in culture. Mass spectrometry analysis of FCHSD2 protein complexes identified multiple interacting proteins that are involved in adhesion and endosome trafficking. We identified and confirmed a novel interaction between FCHSD2 and sorting nexin 18 (SNX18), a BAR domain protein that binds to endosomes. Our results suggest that FCHSD2 is involved in regulating cellular adhesion and cell death.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:OTU.1807/25815 |
| Date | 11 January 2011 |
| Creators | Sue, Stephanie Louise |
| Contributors | Mak, Tak Wah |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | en_ca |
| Detected Language | English |
| Type | Thesis |
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