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Visualization of Bcl‐2 Family Proteins (BIK and BAK) Interactions Using Fluorescence Microscopy
Author(s) -
Kumarjiguda Deepa,
Normand Caitlyn,
RoeckleinCanfield Jennifer
Publication year - 2015
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.29.1_supplement.718.15
Subject(s) - apoptosis , microbiology and biotechnology , programmed cell death , biology , cell , fluorescence microscope , bcl 2 family , virus , cancer cell , oncovirus , cancer , virology , genetics , fluorescence , quantum mechanics , physics
Kaposi's sarcoma is a skin cancer that results in lesions all over the body. Human Herpesvirus 8 (HHV8) is an oncovirus that causes Kaposi's sarcoma. There has long been a link between virus‐encoded proteins that disrupt host cell signaling pathways and cancer in the human host. Programmed cell death, or apoptosis, is an important cellular pathway that halts unreasonable cell growth and disruption of this pathway can lead to tumor development. The human Bcl‐2 family of proteins is involved in both pro and anti apoptotic signals. KSHV expresses a Bcl‐2 homolog, vBcl‐2, which has been shown to inhibit apoptosis in the host cell by several mechanisms. Previous studies and our work have shown a physical interaction between a human pro‐apoptotic protein, Bik, and the KSHV vBcl2 protein, suggesting this interaction is relevant in the anti‐apoptotic function of the virus. Understanding the functional role of this interaction will help elucidate the complex mechanism used by the virus to escape the normal cell death process. We have analyzed this interaction by look at the binding interface in several mutant BIK proteins and their localization in the cell. These interactions are visualized by using fluorescence microscopy. Determining the location of these host proteins during viral infection and expression of vBcl2 is critical to understanding the role the vBcl2‐hBIK interactions plays in apoptosis.