
109 Zina Pitcher pl, 3067 BSRB
Ann Arbor, MICHIGAN 48109
Available to mentor

Ajit is a biologist who trained as an engineer. He received his B.E. in Mechanical engineering from the University of Pune, in India. He conducted doctoral research under the guidance of Prof. Alan Hunt and Prof. Edgar Meyhofer, receiving a Ph.D. in Biomedical Engineering in 2004. He pursued post-doctoral research under the guidance of Prof. Edward Salmon and Prof. Kerry Bloom at the University of North Carolina, Chapel Hill. Ajit joined the Cell and Developmental Biology department as an Assistant Professor. He was promoted to Professor in 2022. Ajit also holds adjunct appointments in the departments of Biophysics and Biomedical Engineering at the University of Michigan.
Joglekar lab
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Postdoctoral fellowshipUniversity of North Carolina at Chapel Hill, Biology, 2010
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Center MemberRogel Cancer Center
Over five decades of research have uncovered most of the molecular machinery that executes cell division. Reductionist approaches have been essential in tackling the complexity of this machinery. However, complex processes such as mitosis also rely on emergent functions. We aim to discover emergent mechanisms of the mitotic machinery using an integrative approach. We engineer novel tools and techniques to enable quantitative investigations of mitotic events in live cells. We use these quantitative data to build mechanistic, mathematical models to gain a deeper understanding of the biology and the biological design of the complex cell division machinery. Currently, there are two major research themes in the Joglekar lab. We are investigating the systems biology of the Mitotic Checkpoint, which is the cell cycle control that ensures accurate chromosome segregation. We are developing novel assays to quantitate the biochemical signaling cascade underlying the mitotic checkpoint and build a detailed mathematical model that describes the signaling dynamics of the checkpoint. This quantitative, mechanistic description of the mitotic checkpoint will allow us to understand and predict its perturbation in cancer cells. Under the second exciting theme, we will reverse engineer the yeast kinetochore – the macromolecular machine that moves chromosomes, using de novo-designed proteins.
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Virdi A, Joglekar AP. 2025 Jan 24;PreprintCell-APP: A generalizable method for microscopic cell annotation, segmentation, and classification.
DOI:10.1101/2025.01.23.634498 PMID: 39896521 -
Chen C, Piano V, Alex A, Han SJY, Huis in ’t Veld PJ, Roy B, Fergle D, Musacchio A, Joglekar AP. Nature Communications, 2023 Dec 1; 14 (1):Journal ArticleThe structural flexibility of MAD1 facilitates the assembly of the Mitotic Checkpoint Complex
DOI:10.1038/s41467-023-37235-z PMID: 36934097 -
Jema S, Chen C, Humphrey L, Karmarkar S, Ferrari F, Joglekar AP. Current Biology, 2023 Oct 23; 33 (20): 4505 - 4515.e4.Journal ArticleSignaling protein abundance modulates the strength of the spindle assembly checkpoint
DOI:10.1016/j.cub.2023.08.074 PMID: 37738972 -
Banerjee A, Chen C, Humphrey L, Tyson JJ, Joglekar AP. Molecular Biology of the Cell, 2022 Sep 1; 33 (10):Journal ArticleBubR1 recruitment to the kinetochore via Bub1 enhances spindle assembly checkpoint signaling
DOI:10.1091/mbc.E22-03-0085 PMID: 35767360 -
Roy B, Han SJY, Fontan AN, Jema S, Joglekar AP. Current Biology, 2022 Jan 10; 32 (1): 237 - 247.e6.Journal ArticleAurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling
DOI:10.1016/j.cub.2021.10.049 PMID: 34861183 -
Roy B, Sim J, Han SJY, Joglekar AP. Open Biology, 2022 Jan 1; 12 (1):Journal ArticleKre28-Spc105 interaction is essential for Spc105 loading at the kinetochore
DOI:10.1098/rsob.210274 PMID: 35042402 -
Chen C, Humphrey L, Jema S, Karmarkar S, Ferrari F, Joglekar A. 2022 May 21; bioRxiv,PreprintSignaling protein abundance modulates the strength of the Spindle Assembly Checkpoint
DOI:10.1101/2022.05.10.491369 -
Chen C, Piano V, Alex A, Han S, In ’t Veld PH, Roy B, Musacchio A, Joglekar A. 2022 Jul 2; bioRxiv,PreprintThe Structural Flexibility of MAD1 Facilitates the Assembly of the Mitotic Checkpoint Complex
DOI:10.1101/2022.06.29.498198