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Cell Biology and the 2016 Nobel Prize in Physiology or Medicine

Five Novel laureates image with the DeltaVision Elite

The 2016 Nobel Prize in Physiology or Medicine was awarded to Yoshinori Ohsumi of the Tokyo Institute of Technology

Who was it awarded to?

The 2016 Nobel Prize in Physiology or Medicine was awarded to Yoshinori Ohsumi of the Tokyo Institute of Technology. Dr. Ohsumi took the road less traveled in his scientific career by selecting a research topic that was not well known in the scientific community when he started his independent research. Today, the field of autophagy is a highly respected research field.

What did Dr. Ohsumi discover?

Dr. Ohsumi performed a genetic screen and identified 15 genes involved in the process of autophagy, which literally means “self- eating.” Autophagy is a cellular recycling system to break down cellular structures into their individual components so that they can be reused. For example, most of us ingest less than 100g of protein a day, but we need to replace two to three times that, and that is where autophagy comes into play. Dr. Ohsumi’s early work focused on discovering genes involved in autophagy and later evolved into detailed functional characterization of these genes. Thanks to the work of Ohsumi and others, we now understand that autophagy is a fundamental cellular process and misregulation of it is associated with cancer, type 2 diabetes, Parkinson’s disease as well as other neurological disorders.

Why basic science is critical for advances in medicine

DeltaVision Elite images yeast in publications from five Nobel laureates

In the past 15 years, the Nobel Prize in Physiology or Medicine was awarded to yeast researchers three times (Hartwell, Hunt, and Nurse in 2001, Rothman, Scheckman, and Südhof in 2011 and Ohsumi in 2016). But, you may ask, “why were yeast researchers awarded the Nobel Prize in Physiology or Medicine?” Besides choosing yeast as their model organism, all three groups used the power of yeast genetics to identify a set of genes involved in a fundamental cell process that when misregulated lead to human disease. Hartwell, Hunt and Nurse discovered cell cycle genes that when not properly regulated can lead to cancer, while Rothman, Scheckman, and Südhof identified genes that regulate vesicle traffic where disruptions lead to immunological disorders, and neurological diseases. Dr. Ohsumi identified genes critical to autophagy; mutations in these genes are associated with neurological diseases and cancer. Identification of genes required for the cell cycle as well as vesicle trafficking and autophagy pathways opened doors for discoveries in higher model organisms as well as in understanding human disease. In other words, fundamental discoveries in basic science paved the way for other researchers to advance our understanding of human disease and to develop novel treatments.

How did GE play a role?

Five of the seven labs that were awarded the three Nobel prizes used the DeltaVision microscope in their published work, including Dr. Hartwell, Dr. Scheckman, Dr. Südhof, Dr. Nurse, and Dr. Ohsumi. The published work spanned the time period of 1997 to 2016 and included prestigious journals such as Cell, Nature, and Nature Communications.

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DeltaVision Elite publications from recent Nobel Prize winners

Castagnetti, S. et al. Fission yeast cells undergo nuclear division in the absence of spindle microtubules. PLoS Biol 8(10), e1000512 (2010), doi: 10.1371/journal.pbio.1000512.

Castagnetti, S. et al. Microtubules offset growth site from the cell centre in fission yeast. J Cell Sci 120(Pt 13), 2205-2213 (2007), doi: 10.1242/jcs.03464.

Coudreuse, D. et al. Driving the cell cycle with a minimal CDK control network. Nature 468(7327), 1074-1079 (2010), doi: 10.1038/nature09543.

Daga, R. et al. Interphase microtubule bundles use global cell shape to guide spindle alignment in fission yeast. J Cell Sci 121(12), 1973-1980 (2008), doi: 10.1242/jcs.011825.

Ge, L. et al. Phosphatidylinositol 3-kinase and COPII generate LC3 lipidation vesicles from the ER-Golgi intermediate compartment. eLIFE 3(e04135), 1-13 (2014), doi: 10.7554/eLife.04135.

Gutiérrez-Escribano, P. et al. A single cyclin-CDK complex is sufficient for both mitotic and meiotic progression in fission yeast. Nat Commun 6(6871), 1-13 (2015), doi: 10.1038/ncomms7871.

Hamasaki, M. et al. Starvation triggers the delivery of the endoplasmic reticulum to the vacuole via autophagy in yeast. Traffic 6(1), 56-65 (2005), doi: 10.1111/j.1600-0854.2004.00245.x.

Hamasaki, M. et al. The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct 28(1), 49-54 (2003), doi: 10.1247/csf.28.49.

Juardo, S. LTP requires a unique postsynaptic SNARE fusion machinery. Neuron 77(3), 542-558 (2013), doi: 10.1016/j.neuron.2012.11.029.

Kabeya, Y. et al. LC3, GABARAP, and GATE16 localize to autophagosomal membrane depending on form-II formation. J Cell Sci 117(13), 2805-2812 (2004), doi: 10.1242/jcs.01131.

Kawamata, T. et al. Characterization of a novel autophagy-specific gene, ATG29. Biochem Biophys Res Commun 338(4), 1884-1889 (2005), doi: 10.1016/j.bbrc.2005.10.163.

Kaykov, A. et al. The spatial and temporal organization of origin firing during the S-phase of fission yeast. Genome Res 25(3), 391-401 (2015), doi: 10.1101/gr.180372.114.

Kelly, F. et al. De novo growth zone formation from fission yeast spheroplasts. PLoS One 6(12), e27977 (2011), doi: 10.1371/journal.pone.0027977.

Kelly, F. et al. Spatial control of Cdc42 activation determines cell width in fission yeast. Mol Biol Cell 22(20), 3801-3811 (2011), doi: 10.1091/mbc.E11-01-0057.

Mizushima, N. et al. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 152(4), 657-668 (2001), doi: 10.1083/jcb.152.4.657.

Mizushima, N. et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J Cell Sci 116(9), 1679-1688 (2003), doi: 10.1242/jcs.00381.

Moseley, J. et al. A spatial gradient coordinates cell size and mitotic entry in fission yeast. Nature, 459(7248), 857-860 (2009), doi: 10.1038/nature08074.

Onodera, J. et al. Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae. J Biol Chem 279(16), 16071-16076 (2004), doi: 10.1074/jbc.M312706200.

Pardo, M. et al. The nuclear rim protein Amo1 is required for proper microtubule cytoskeleton organization in fission yeast. J Cell Sci 118(8), 1705-1714 (2005), doi: 10.1242/jcs.02305.

Shimazu, M. et al. A family of basic amino acid transporters of the vacuolar membrane from Saccharomyces cerevisiae. J Biol Chem 280(6), 4851-4857 (2005), doi: 10.1074/jbc.M412617200.

Shintani, T. et al. Apg2p functions in autophagosome formation on the perivacuolar structure. J Biol Chem 32(10), 30452-30460 (2001), doi: 10.1074/jbc.M102346200.

Suzuki, K. et al. Interrelationships among Atg proteins during autophagy in Saccharomyces cerevisiae. Yeast 21(12), 1057-1065 (2004), doi: 10.1002/yea.1152.

Suzuki, K. et al. Studies of cargo delivery to the vacuole mediated by autophagosomes in Saccharomyces cerevisiae. Dev Cell 3(6), 815-824 (2002), doi: 10.1016/S1534-5807(02)00359-3.

Suzuki, K. et al. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO 20(21), 5971-5981 (2001), doi: 10.1093/emboj/20.21.5971.

Takemoto, A. et al. Nuclear envelope expansion is crucial for proper chromosomal segregation during a closed mitosis. J Cell Sci 129(6), 1250-1259 (2016), doi: 10.1242/jcs.181560.

Toczyski, D. et al. CDC5 and CKII control adaptation to the yeast DNA damage checkpoint. Cell 90(6), 1097-1106 (1997), doi: 10.1016/S0092-8674(00)80375-X.

Wood, E. et al. Pom1 and cell size homeostasis in fission yeast. Cell Cycle 12(19), 3228-3236 (2013), doi: 10.4161/cc.26462.

Wuarin, J. et al. Stable association of mitotic Cyclin B/Cdc2 to replication origins prevents endoreduplication. Cell 111(3), 419-431 (2002), doi: 10.1016/S0092-8674(02)01042-5.

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