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Rajat Rohatgi
Medical oncologist, Thoracic specialist
Associate Professor of Biochemistry and of Medicine (Oncology)
Practice Areas
Professional Education
- Fellowship: Stanford University - CAPS (2008) CA
- Residency: Stanford University - CAPS (2004) CA
- Board Certification: Medical Oncology, American Board of Internal Medicine (2008)
- Board Certification: Internal Medicine, American Board of Internal Medicine (2005)
- Medical Education: Harvard Medical School (2002) MA
- Fellowship, Stanford Hospital, Medical Oncology (2008)
- Residency, Stanford Hospital, Internal Medicine (2004)
- Ph.D., Harvard Medical School, Cell Biology (2002)
- M.D., Harvard Medical School (2002)
- A.B., Harvard University, Biochemical Sciences (1994)
Honors & Awards
- Fellowship Award, Damon Runyon Cancer Research Fund (2006)
- Young Investigator Award, American Society for Clinical Oncology (2007)
- Howard Temin Pathway to Independance Award (K99/R00), NCI/NIH (2007)
- Josephine Q. Berry Faculty Scholar in Cancer Research, Stanford University (2009)
- Martin D. Abeloff Scholar, V Foundation for Cancer Research (2009-2011)
- Stand Up To Cancer Innovation Research Grant, American Association for Cancer Research (2010-2013)
- Basil O' Connor Starter Scholar Award, March of Dimes Foundation (2010-2012)
- Distinguished Scientist Award, Sontag Foundation (2010)
- NIH Director's New Innovator Award, NIH (2012)
Publications
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EFCAB7 and IQCE Regulate Hedgehog Signaling by Tethering the EVC-EVC2 Complex to the Base of Primary Cilia
Pusapati, G. V., Hughes, C. E., Dorn, K. V., Zhang, D., Sugianto, P., & Rohatgi, R. (2014). EFCAB7 and IQCE Regulate Hedgehog Signaling by Tethering the EVC-EVC2 Complex to the Base of Primary Cilia. DEVELOPMENTAL CELL, 28(5), 483-496. -
Gli Protein Activity Is Controlled by Multisite Phosphorylation in Vertebrate Hedgehog Signaling
Niewiadomski, P., Kong, J. H., Ahrends, R., Ma, Y., Humke, E. W., & Rohatgi, R. (2014). Gli Protein Activity Is Controlled by Multisite Phosphorylation in Vertebrate Hedgehog Signaling. CELL REPORTS, 6(1), 168-181. -
Structure and function of the Smoothened extracellular domain in vertebrate Hedgehog signaling
Nachtergaele, S., Whalen, D. M., Mydock, L. K., Zhao, Z., Malinauskas, T., & Rohatgi, R. (2013). Structure and function of the Smoothened extracellular domain in vertebrate Hedgehog signaling. ELIFE, 2. -
A Smoothened-Evc2 Complex Transduces the Hedgehog Signal at Primary Cilia
Dorn, K. V., Hughes, C. E., & Rohatgi, R. (2012). A Smoothened-Evc2 Complex Transduces the Hedgehog Signal at Primary Cilia. DEVELOPMENTAL CELL, 23(4), 823-835.
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Oxysterols are allosteric activators of the oncoprotein Smoothened
Nachtergaele, S., Mydock, L. K., Krishnan, K., Rammohan, J., Schlesinger, P. H., & Rohatgi, R. (2012). Oxysterols are allosteric activators of the oncoprotein Smoothened. NATURE CHEMICAL BIOLOGY, 8(2), 211-220.
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The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins
Humke, E. W., Dorn, K. V., Milenkovic, L., Scott, M. P., & Rohatgi, R. (2010). The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins. GENES & DEVELOPMENT, 24(7), 670-682.
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Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium
Milenkovic, L., Scott, M. P., & Rohatgi, R. (2009). Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium. JOURNAL OF CELL BIOLOGY, 187(3), 365-374.
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Hedgehog signal transduction by smoothened: pharmacological evidence for a two-step activation process.
Rohatgi R, M. L., Corcoran RB, & Scott MP. (2009). Hedgehog signal transduction by smoothened: pharmacological evidence for a two-step activation process. Proceedings of the National Academy of Sciences USA, 106.
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Patched1 regulates Hedgehog signaling at the primary cilium.
Rohatgi R, M., & Scott MP. (2007). Patched1 regulates Hedgehog signaling at the primary cilium. Science, 317(5836).
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Location, location, and location: compartmentalization of Hedgehog signaling at primary cilia.
Pusapati, G. V., & Rohatgi, R. (2014). Location, location, and location: compartmentalization of Hedgehog signaling at primary cilia. EMBO journal, 33(17), 1852-1854.
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G-protein-coupled receptors, Hedgehog signaling and primary cilia
Mukhopadhyay, S., & Rohatgi, R. (2014). G-protein-coupled receptors, Hedgehog signaling and primary cilia. SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 33, 63-72.
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A Novel Osteogenic Oxysterol Compound for Therapeutic Development to Promote Bone Growth: Activation of Hedgehog Signaling and Osteogenesis Through Smoothened Binding
Montgomery, S. R., Nargizyan, T., Meliton, V., Nachtergaele, S., Rohatgi, R., & Parhami, F. (2014). A Novel Osteogenic Oxysterol Compound for Therapeutic Development to Promote Bone Growth: Activation of Hedgehog Signaling and Osteogenesis Through Smoothened Binding. JOURNAL OF BONE AND MINERAL RESEARCH, 29(8), 1872-1885.
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Tracking the Subcellular Fate of 20( S)-Hydroxycholesterol with Click Chemistry Reveals a Transport Pathway to the Golgi
Peyrot, S. M., Nachtergaele, S., Luchetti, G., Mydock-McGrane, L. K., Fujiwara, H., & Rohatgi, R. (2014). Tracking the Subcellular Fate of 20( S)-Hydroxycholesterol with Click Chemistry Reveals a Transport Pathway to the Golgi. JOURNAL OF BIOLOGICAL CHEMISTRY, 289(16), 11095-11110.
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Isolation and mutational analysis of circulating tumor cells from lung cancer patients with magnetic sifters and biochips
Earhart, C. M., Hughes, C. E., Gaster, R. S., Ooi, C. C., Wilson, R. J., & Wang, S. X. (2014). Isolation and mutational analysis of circulating tumor cells from lung cancer patients with magnetic sifters and biochips. LAB ON A CHIP, 14(1), 78-88.
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Isolation and mutational analysis of circulating tumor cells from lung cancer patients with magnetic sifters and biochips.
Earhart, C. M., Hughes, C. E., Gaster, R. S., Ooi, C. C., Wilson, R. J., & Wang, S. X. (2013). Isolation and mutational analysis of circulating tumor cells from lung cancer patients with magnetic sifters and biochips. Lab on a chip, 14(1), 78-88.
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Cancer Risk After Use of Recombinant Bone Morphogenetic Protein-2 for Spinal Arthrodesis
Carragee, E. J., Chu, G., Rohatgi, R., Hurwitz, E. L., Weiner, B. K., & Kopjar, B. (2013). Cancer Risk After Use of Recombinant Bone Morphogenetic Protein-2 for Spinal Arthrodesis. JOURNAL OF BONE AND JOINT SURGERY-AMERICAN VOLUME, 95A(17), 1537-1545.
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Chemically inducible diffusion trap at cilia reveals molecular sieve-like barrier.
Lin, Y.-C., Niewiadomski, P., Lin, B., Nakamura, H., Phua, S. C., & Inoue, T. (2013). Chemically inducible diffusion trap at cilia reveals molecular sieve-like barrier. Nature chemical biology, 9(7), 437-443.
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Singapore signalling: the 2012 hedgehog pathway cocktail
Briscoe, J., & Rohatgi, R. (2012). Singapore signalling: the 2012 hedgehog pathway cocktail. EMBO REPORTS, 13(7), 580-583.
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Cilia 2010: The Surprise Organelle of the Decade
Smith, E. F., & Rohatgi, R. (2011). Cilia 2010: The Surprise Organelle of the Decade. SCIENCE SIGNALING, 4(155).
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The ciliary membrane
Rohatgi, R., & Snell, W. J. (2010). The ciliary membrane. CURRENT OPINION IN CELL BIOLOGY, 22(4), 541-546.
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Role of Lipid Metabolism in Smoothened Derepression in Hedgehog Signaling
Yavan, A., Nagaraj, R., Owusu-Ansah, E., Folick, A., Ngo, K., & Banerjee, U. (2010). Role of Lipid Metabolism in Smoothened Derepression in Hedgehog Signaling. DEVELOPMENTAL CELL, 19(1), 54-65.
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Arrestin? Movement in Cilia.
Rohatgi R, & Scott MP. (2008). Arrestin? Movement in Cilia. Science, 320(5884).
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Patching the gaps in Hedgehog signaling.
Rohatgi R, & Scott MP. (2007). Patching the gaps in Hedgehog signaling. Nat Cell Bio, 9(9).
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In vitro reconstitution of cdc42-mediated actin assembly using purified components.
Ho HY, Rohatgi R, Lebensohn A, & Kirschner MW. (2006). In vitro reconstitution of cdc42-mediated actin assembly using purified components. Methods in Enzymology, 406.
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Loss-of-function Analysis of EphA Receptors in Retinotectal mapping.
Feldheim DA, Nakamoto M, Osterfield M, Gale NW, DeChiara TM, & Flanagan JG. (2004). Loss-of-function Analysis of EphA Receptors in Retinotectal mapping. Journal of Neuroscience, 24(10).
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Toca-1 Mediates Cdc42- Dependent Actin Nucleation by Activating the N-WASP-WIP Complex.
Ho HY, R. R., Lebensohn A, Ma L, Li L, Gygi SP, & Kirschner MW. (2004). Toca-1 Mediates Cdc42- Dependent Actin Nucleation by Activating the N-WASP-WIP Complex. Cell, 118(2).
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The Mechanism of Regulation of WAVE1-induced Actin Nucleation by Rac1 and Nck.
Eden S, Rohatgi R, Podtelejnikov AV, Mann M, & Kirschner MW. (2002). The Mechanism of Regulation of WAVE1-induced Actin Nucleation by Rac1 and Nck. Nature, 418(6899).
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Nck and Phosphatidylinositol 4,5 Bisphosphate Synergistically Activate Actin Polymerization Through the N-WASP-Arp2/3 Pathway.
Rohatgi R, Nollau P, Ho HY, Kirschner MW, & Mayer BJ. (2001). Nck and Phosphatidylinositol 4,5 Bisphosphate Synergistically Activate Actin Polymerization Through the N-WASP-Arp2/3 Pathway. Journal of Biological Chemistry, 276(28).
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CR16 Forms a Complex with N-WASP in Brain and is a Novel Member of a Conserved Proline-Rich Actin-Binding Protein Family.
Ho HY, R. R., Ma L, & Kirschner MW. (2001). CR16 Forms a Complex with N-WASP in Brain and is a Novel Member of a Conserved Proline-Rich Actin-Binding Protein Family. Proceedings of the National Academy of Sciences USA, 98(20).
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WIP Regulates N-WASP-Mediated Actin Polymerization and Filopodium Formation.
Martinez-Quiles N, Rohatgi R, Anton IM, Medina M, Saville SP, & Ramesh N. (2001). WIP Regulates N-WASP-Mediated Actin Polymerization and Filopodium Formation. Nature Cell Biology, 3(5).
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Mechanism of N-WASP Activation by CDC42 and Phosphatidylinositol 4, 5-Bisphosphate.
Rohatgi R, H. Hy., & Kirschner MW. (2000). Mechanism of N-WASP Activation by CDC42 and Phosphatidylinositol 4, 5-Bisphosphate. Journal of Cell Biology, 150(6).
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The Interaction Between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin Assembly.
Rohatgi R, M. L., Miki H, Lopez M, Kirchhausen T, Takenawa T, & Kirschner MW. (1999). The Interaction Between N-WASP and the Arp2/3 Complex Links Cdc42-Dependent Signals to Actin Assembly. Cell, 97(2).
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The Arp2/3 Complex Mediates Actin Polymerization Induced by the Small GTP-Binding Protein Cdc42.
Ma L, Rohatgi R, & Kirschner MW. (1998). The Arp2/3 Complex Mediates Actin Polymerization Induced by the Small GTP-Binding Protein Cdc42. Proceedings of the National Academy of Sciences USA, 95(26).
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Non-Enzymatic, Template-Directed Ligation of Oligoribonucleotides is Highly Regioselective for the Formation of 3'-5'-Phosphodiester Bonds
Rohatgi R, Bartel DP, & Szostak JW. (1996). Non-Enzymatic, Template-Directed Ligation of Oligoribonucleotides is Highly Regioselective for the Formation of 3'-5'-Phosphodiester Bonds. Journal of the American Chemical Society, 118(14).
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Kinetic and Mechanistic Analysis of Non-Enzymatic, Template-Directed Oligoribonucleotide Ligation.
Rohatgi R, Bartel DP, & Szostak JW. (1996). Kinetic and Mechanistic Analysis of Non-Enzymatic, Template-Directed Oligoribonucleotide Ligation. Journal of the American Chemical Society, 118(14).
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