Charles E. Samuel
Awards / Honors
- National Institutes of Health Research Career Development Award
- National Institute of Allergy and Infectious Diseases MERIT Award
- FASEB Wellcome Professorship Award
- Humboldt Forschungspreis Award
- Virology Editorial Board (1980-2012)
- Journal of Interferon and Cytokine Research Editorial Board (1980-2014); Associate Editor (2014- )
- Journal of Virology Editorial Board (1984-95, 2006- )
- Journal of Biological Chemistry Editorial Board (1989-93, 1996-2000); Associate Editor (2002- )
- Elected Fellow, American Association for the Advancement of Science (2006)
- Elected Member, American Academy of Microbiology (2007)
- President, Internat. Society Interferon & Cytokine Res (2012-2013)
- 62nd Annual Faculty Research Lecturer, U.C. Santa Barbara (2017)
Charles Samuel is the C. A. Storke II Professor. He earned a B.S. in Chemistry from Montana State and his Ph.D. in Biochemistry from U.C. Berkeley. He was a Damon Runyon Scholar at Duke Univ. Med. Sch. where he began work on interferon. At UCSB he served as Director of the Interdepartmental Biochemistry & Molecular Biology Program (BMSE) from 1987-95, as Founding Chair of the Department of Molecular, Cellular & Developmental Biology from 1995-98, and again as MCDB Chair from 2001-04. He is an NIH Research Career Development Awardee, an NIH MERIT awardee, a FASEB Wellcome Professorship awardee, a Humboldt Forschungspreis recipient, and an elected Fellow of the American Association for the Advancement of Science and the American Academy of Microbiology. He is an Associate Editor of the Journal of Biological Chemistry, and Journal of Interferon and Cytokine Research, and serves on the editorial board of Journal of Virology.
The overall objective of the research in The Samuel Lab is to elucidate in molecular terms the mechanisms by which interferons exert their antiviral and cell growth control actions in mammalian cells. Present work includes biochemical and molecular genetic studies of two interferon-inducible enzymes, PKR and ADAR. PKR is a double-stranded RNA-dependent protein kinase induced by IFN, and activated by RNA-dependent autophosphorylation. PKR plays a major role in the regulation of translation of viral and cellular mRNAs and also modulates transcription and signaling. The ADAR1 deaminase is an RNA editing-enzyme that catalyzes the C-6 deamination of adenosine to yield inosine, thereby altering the genetic decoding and structure of RNAs. While PKR displays antiviral and proapoptic activities, ADAR1 is often proviral and antiapoptotic in virus-infected cells. Furthermore, PKR is not required for normal mouse embryogenesis, whereas ADAR1 is required.
Tan,M.H., Li,Q., Shanmugam,R., Piskol,R., Kohler, J., et al. (2017) Dynamic landscape and regulation of RNA editing in mammals. Nature 550(7675):249-254.
Ma, D, George C.X., Nomburg, J., Pfaller, C.K., Cattaneo, R., and Samuel, C.E. (2017). Upon infection the cellular WD repeat-containing protein 5 localizes to cytoplasmic inclusion bodies and enhances measles virus replication. J. Virol.: in press.
George, C.X., Ramaswami, G., Li, J.B., Samuel, C.E. (2016) Editing of cellular self-RNAs by adenosine deaminase ADAR1 suppresses innate immune stress responses. J Biol Chem. 291:6158-68.
Kainulainen, M., Lau, S., Samuel, C.E., Hornung, V., Weber, F. (2016) NSs virulence factor of Rift Valley Fever Virus engages the F-box proteins FBXW11 and Î²-TRCP1 to degrade the antiviral protein kinase PKR. J Virol. 90:6140-6147.
George, C. X., Samuel, C. E. (2015) STAT2-dependent induction of RNA adenosine deaminse ADAR1 by type 1 interferon differs between mouse and human cells in the requirement for STAT1. Virology 485: 363-370.
Pfaller, C. K., Mastorakos, G.M., Matchett, W.E., Ma, X., et al. (2015) Measles virus defective interfering RNAs are generated frequently and early in the absence of C protein and can be destabilized by adenosine deaminase actiing on RNA1-like hypermutations. J. Virol. 89: 7735-7747.
George, C.X., John, L., Samuel, C.E. (2014) An RNA Editor, Adenosine Deaminase Acting on Double-Stranded RNA (ADAR1). J. Interferon Cytokine Res. 34:437-46.
Pfaller, C.K., Radeke, M.J., Cattaneo, R., Samuel, C.E. (2014) Measles virus C protein impairs production of defective copyback double-stranded viral RNA and activation of protein kinase R. J. Virol. 88:456-68.
John, L., Samuel, C.E. (2014) Induction of stress granules by interferon and down-regulation by the cellular RNA adenosine deaminase ADAR1. Virology 454-455:299-310.
Okonski, K.M., Samuel, C.E. (2013) Stress Granule Formation Induced by Measles Virus is Protein Kinase PKR-dependent and Impaired by RNA Adenosine Deaminase ADAR1. J. Virol. 87: 756-766
Taghavi, N., Samuel, C.E. (2013) RNA-dependent protein kinase PKR and the Z-DNA binding orthologue PKZ differ in their capacity to mediate initiation factor eIF2-dependent inhibition of protein synthesis and virus-induced stress granule formation. Virology 443: 48-58.
McAllister, C.S., Taghavi, N., Samuel, C.E. (2012) Protein Kinase PKR Amplification of Interferon β Induction Occurs through Initiation Factor eIF-2α-mediated Translational Control. J. Biol. Chem. 287:36384-36392.
Ruggieri A, Dazert E, Metz P, Hofmann S, Bergeest JP, Mazur J, et al. (2012) Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection. Cell Host Microbe 12:71-85.
Li, Z., Okonski, K. M., and Samuel, C. E. (2012) Adenosine Deaminase Acting on RNA 1 (ADAR1) Suppresses the Induction of Interferon by Measles Virus. J Virol. 86: 3787-3794.
Samuel CE (2012) Understanding human Immunodeficiency virus-host interactions at the biochemical level. J. Biol. Chem. 287: 40838-40840.
Taghavi, N., and Samuel C. E. (2012) Protein kinase PKR catalytic activity is required for the PKR-dependent activation of mitogen-activated protein kinases and amplification of interferon beta induction following virus infection. Virology 427: 208-216.
Samuel, C.E. (2011) Adenosine Deaminases Acting on RNAs (ADARs) are both Antiviral and Proviral. Virology 411: 180-193.
Ward, S.V., George, C.X., Welch,M.J., Liou, L-Y, Hahm, B., Lewicki, H, de la Torre, J.C., Samuel, C.E., and Oldstone, M.B. (2011) RNA Editing Enzyme Adenosine Deaminase is a Restriction Factor for Controlling Measles Virus Replication that also is Required for Embryogenesis. Proc. Natl. Acad. Sci. USA 108: 331-336.
George, C.X., and Samuel, C.E. (2011) Host Response to Polyoma Virus Infection is Modulated by RNA Adenosine Deaminse ADAR1 but not by ADAR2. J. Virol. 85: 8338-8347.
Bouxsein, N.F., Leal, C., McAllister, C.S., Ewert, K.K., Li, Y., Samuel, C.E., and Safinya, C.S. (2011) Two-dimensional Packing of Short DNA with Non-pairing Overhangs in Cationic Liposome-DNA Complexes: From Onsager Nematics to Columnar Nematics with Finite-length Columns. J. Am. Chem. Soc. 133: 7585-7595.
Pfaller CK, Li Z, George CX, Samuel CE. (2011) Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response. Curr Opin Immunol. 23: 573-582
McAllister, C.S., Toth, A.M., Zhang, P., Devaux, P., Cattaneo, R., and Samuel, C.E. (2010) Mechanisms of Protein Kinase PKR-mediated Amplification of Beta Interferon Induction by C Protein-deficient Measles Virus. J. Virol. 84 : 380-386.
Li, Z., Wolff, K.C., and Samuel, C.E. (2010) RNA Adenosine Deaminase ADAR1 Deficiency Leads to Increased Activation of Protein Kinase PKR and Reduced Vesicular Stomatitis Virus Growth following Interferon Treatment. Virology 396: 316-322.
Toth, A.M., Li, Z., Cattaneio, R., and Samuel, C.E. (2009) RNA-specific adenosine deaminae ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR. J. Biol. Chem. 284: 29350-29356.
Zhang, P., Langland, J.O., Jacobs, B.L., Samuel, C.E. (2009) Protein kinase PKR-dependent activation of mitogen-activated protein kinases occurs through mitochondrial adapter IPS-1 and is antagonized by vaccinia virus E3L. J. Virol. 83: 5718-5725.
McAllister, C.S., Samuel, C.E. (2009) Protein kinase PKR enhances the induction of interferon-beta and apoptosis mediated by cytoplasmic RNA sensors. J. Biol. Chem. 284: 1644-1651.