- Highlights
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News highlights in February 2010
All you need to know when studying autophagy
Recently years have witnessed the explosive interests in autophagy in biology. Autophagy, originally considered as a simple catabolic process, has been implicated in various diseases including cancer, neurodegenerative disease, infectious disease and cardiovascular disease. Despite the rapid progression in deciphering functional roles of autophagy in pathology, the technical development to detect and quantify autophagy is lagging. Autophagy, as a dynamic process, is particularly difficult to quantify and the experimental data are frequently subjected to misinterpretations.
A recent review article in Cell provides all possible means to examine autophagy. The cons and pros of each method are discussed in great detail. The paper by Levine and colleagues sets a gold standard in the field of autophagy. Combined with another article in Autophagy by Klionsky and colleagues in 2008, these papers will help to clarify misconceptions and possibly serve as textbook in autophagy study.Reference: Mizushima et al, Cell , February 2010.
Novel approach to rapidly inactivate protein function
Loss-of-function is the most important way to assess the biological roles of favorite genes. Traditional approaches include knockout by homologous recombination, knockdown by siRNA and small inhibitors. While all of them have various limitations, a novel approach presented by Robinson and colleagues can rapidly inactivate protein function with great precision and high reproducibility.
Rapamycin is a cell-permeable small molecule which binds to rapamycin binding domain (RBD). Rapamycin also binds to the FKBP motif. When there two domains are expressed as a fusion protein with other molecules, rapamycin can bridge the interaction of carrier proteins. Robinson et al applied this concept in mammalian cells to examine the role of APs in endocytosis. In cells stably transfected mitochondrial targeted RBD protein, the exogenous AP1 was fused with FKBP and expressed at comparable levels as endogenous AP1 which was knockdowned. Administration of rapamycin triggered the re-routing of AP1 from cytosol to mitochondria in seconds. By studying the trafficking pattern of client molecules, the researchers confirmed the importance of AP1 in retrograde trafficking. This type of approach can also be applied in inactivating other protein under certain circumstances.Reference: Robinson et al, Dev cell , February 2010.
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