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Your persistence has brought you to this milestone. Forever, Go Blue! Different means to the same end: How a worm protects its chromosomes C. elegans protein domains identified by Nandakumar team New in Nature Neuroscience Bo Duan Lab and collaborators identify protein in mammals that senses cold Better Understanding of Science Through Creative Works A nod to the Art-and-Resistance semester: a former student’s ceramics help explain resistance to fluoride ion build up in bacterial cells and offer a novel science communication channel to help us resist misinformation Faculty promoted in 2023 Nandakumar Lab: Not all pot holes are bad In Science report on preventing DNA repair from mishandling telomeres ‘Binocular’ treatment helps with a common vision problem. Sleep makes it stick! New from the Aton Lab Sixteen Research Themes MCDB research follows 16 themes, including Signal Transduction and Communications. This image from the Cadigan lab shows a mutation’s effect on Drosophila antenna. Explore our graduate programs PhD application deadline: Dec. 1 Slide 0 Slide 1 Slide 2 Slide 3 Slide 4 Slide 5 Slide 6 Slide 7 Slide 8 Previous Slide Next Slide Recent News Different means to the same end: How a worm protects its chromosomes In Proceedings of the National Academy of Sciences, JK Nandakumar and his team identify the specific domains in the proteins used by C. elegans a different solution than that used by mammals to protect their telomeres. Researchers uncover protein responsible for cold sensation Nature Neuroscience report from a collaboration of the labs of MCDB’s Bo Duan and LSI’s Shawn Xu fills "a gap in temperature-sensing puzzle" all newsU-M Health Response CAMPUS INFORMATION MCDB Climate Report Form MCDB DEI RESOURCESRecent Publications More Info Simmons Lab: Bacillus subtilis encodes a discrete flap endonuclease that cleaves RNA-DNA hybrids Frances Caroline Crowder, Lyle S. Simmons Abstract The current model for Okazaki fragment maturation in bacteria invokes RNA cleavage by RNase H, followed by strand displacement synthesis and 5′ RNA flap removal by DNA polymerase I (Pol I). RNA removal by Pol I is thought to occur through the 5′-3′ flap endo/exonuclease (FEN) domain, located in the N-terminus of the protein. In addition to Pol I, many bacteria encode a second, Pol I-independent FEN. The contribution of Pol I and Pol I-independent FENs to DNA replication... See More Journal of Biological Chemistry, Volume 298, Issue 7, 2022, 102088 Chapman Lab: Mechanistic insights into accelerated α-synuclein aggregation mediated by human microbiome-associated functional amyloids Sujeet S. Bhoite, Yilin Han, Brandon T. Ruotolo, Matthew R. Chapman Abstract: The gut microbiome has been shown to have key implications in the pathogenesis of Parkinson’s disease (PD). The Escherichia coli functional amyloid CsgA is known to accelerate α-synuclein aggregation in vitro and induce PD symptoms in mice. However, the mechanism governing CsgA-mediated acceleration of α-synuclein aggregation is unclear. Here, we show that CsgA can form stable homodimeric species that correlate with faster α-synuclein amyloid aggregation. Furthermore, we identify and characterize new CsgA homologs encoded by bacteria present in the human microbiome. These CsgA... See More Molecular Cell Sept. 1, 2022 Jakob Lab: From guide to guard—activation mechanism of the stress-sensing chaperone Get3 Kathrin Ulrich, Ákos Farkas, Olivia Chan, Olivia Katamanin, Blanche Schwappach, Ursula Jakob SUMMARY: Oxidative stress conditions can cause ATP depletion, oxidative protein unfolding, and potentially toxic protein aggregation. To alleviate this proteotoxic stress, the highly conserved yeast protein, Get3, switches from its guiding function as an ATP-dependent targeting factor for tail-anchored proteins to its guarding function as an ATP-independent molecular chaperone that prevents irreversible protein aggregation. Here, we demonstrate that activation of Get3’s chaperone function follows a tightly orchestrated multi-step process, centered around the redox status of two... See More Journal of Biological Chemistry, Volume 298, Issue 8, 2022, 102219, Wang Lab: GRASP55 regulates the unconventional secretion and aggregation of mutant huntingtin Erpan Ahat, Sarah Bui, Jianchao Zhang, Felipe da Veiga Leprevost, Lisa Sharkey, Whitney Reid, Alexey I. Nesvizhskii, Henry L. Paulson, Yanzhuang Wang, Abstract: Recent studies demonstrated that the Golgi reassembly stacking proteins (GRASPs), especially GRASP55, regulate Golgi-independent unconventional secretion of certain cytosolic and transmembrane cargoes; however, the underlying mechanism remains unknown. Here, we surveyed several neurodegenerative disease–related proteins, including mutant huntingtin (Htt-Q74), superoxide dismutase 1 (SOD1), tau, and TAR DNA–binding protein 43 (TDP-43), for unconventional secretion; our results show that Htt-Q74 is most robustly secreted in a GRASP55-dependent manner. Using Htt-Q74 as a model system,... See More Journal of Biological Chemistry, Volume 299, Issue 1, 2023 Cadigan Lab: SOX9 and TCF transcription factors associate to mediate Wnt/β-catenin target gene activation in colorectal cancer Aravinda-Bharathi Ramakrishnan, Peter E. Burby, Kavya Adiga, Ken M. Cadigan Abstract: Activation of the Wnt/β-catenin pathway regulates gene expression by promoting the formation of a β-catenin–T-cell factor (TCF) complex on target enhancers. In addition to TCFs, other transcription factors interact with the Wnt/β-catenin pathway at different levels to produce tissue-specific patterns of Wnt target gene expression. The transcription factor SOX9 potently represses many Wnt target genes by downregulating β-catenin protein levels. Here, we find using colony formation and cell growth assays that SOX9 surprisingly promotes the proliferation of Wnt-driven colorectal cancer... See More eLife 11:e78201 DeSantis/Nandakumar Labs: The KASH5 protein involved in meiotic chromosomal movements is a novel dynein activating adaptor Ritvija Agrawal, John P Gillies, Juliana L Zang, Jingjing Zhang, Sharon R Garrott, Hiroki Shibuya, Jayakrishnan Nandakumar, Morgan E DeSantis Dynein harnesses ATP hydrolysis to move cargo on microtubules in multiple biological contexts. Dynein meets a unique challenge in meiosis by moving chromosomes tethered to the nuclear envelope to facilitate homolog pairing essential for gametogenesis. Though processive dynein motility requires binding to an activating adaptor, the identity of the activating adaptor required for dynein to move meiotic chromosomes is unknown. We show that the meiosis-specific...