Christopher P. Hill, DPhil

Co-Chair, Department of Biochemistry

Research Interests

  • Proteasome Activation and Regulation
  • Structural Biology
  • ESCRT Pathway
  • Protein Quality Control
  • HIV Structure and Host Interactions
  • Nucleosome Remodeling and Reorganization

Labs

Lab Website

Languages

  • English

Academic Information

  • Departments: Biochemistry - Distinguished Professor
  • Cancer Center Programs: Nuclear Control of Cell Growth & Differentiation

Academic Office Information

  • 801-585-5536
  • Emma Eccles Jones Research Building
    Biochemistry
    15 North Medical Drive East, Room: 3600A
    Salt Lake City, UT 84112

Academic Bio

Christopher Hill, D.Phil., is a distinguished professor in the Department of Biochemistry at the University of Utah School of Medicine. He serves as department co-chair jointly with Wes Sundquist, holds the H.A. and Edna Benning Medical Society Chair, and is a member of the Nuclear Control of Cell Growth and Differentiation Program.

The Hill Lab uses structural and biochemical approaches to study how proteins function. This approach is applied to numerous targets that are relevant to cancer mechanisms. Studies on proteasome and protein quality control seek to understand mechanisms in a validated cancer therapeutic target. Studies of HIV-host interactions and the ESCRT pathway have led into mechanistic studies on how cells divide, and may inform new approaches to prevent the uncontrolled proliferation characteristic of cancers. Studies on nucleosome remodeling and reorganizing complexes advance understanding of mechanisms of gene expression, which may offer insights to the genetic defects that underlie progression toward cancer.

Hill received his BA and D.Phil. from the University of York, England. He then completed a postdoctoral fellowship at the University of California at Los Angles. Hill presents and publishes widely and has received numerous research fellowships and grants.

Education History

Type School Degree
Postdoctoral Fellowship University of California, Los Angeles
Structural Biology
Postdoctoral Fellow
Postdoctoral Fellowship University of York
Chemistry
Postdoctoral Fellow
Doctoral Training University of York
Chemistry
D.Phil.
Undergraduate University of York
Chemistry
B.A.

Global Impact

Education History

Type School Degree Country
Postdoctoral Fellowship University of York
Chemistry
Postdoctoral Fellow United Kingdom
Doctoral Training University of York
Chemistry
D.Phil. United Kingdom
Undergraduate University of York
Chemistry
B.A. United Kingdom

Selected Publications

Journal Article

  1. FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.Kemble DJ, McCullough LL, Whitby FG, Formosa T, Hill CP (2015). FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs. Mol Cell, 60(2), 294-306.
  2. Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets.Clinton TR, Weinstock MT, Jacobsen MT, Szabo-Fresnais N, Pandya MJ, Whitby FG, Herbert AS, Prugar LI, McKinnon R, Hill CP, Welch BD, Dye JM, Eckert DM, Kay MS (2015). Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets. Protein Sci, 24(4), 446-63.
  3. Structural basis for the activation and inhibition of the UCH37 deubiquitylase.VanderLinden RT, Hemmis CW, Schmitt B, Ndoja A, Whitby FG, Robinson H, Cohen RE, Yao T, Hill CP (2015). Structural basis for the activation and inhibition of the UCH37 deubiquitylase. Mol Cell, 57(5), 901-11.
  4. Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).Han H, Monroe N, Votteler J, Shakya B, Sundquist WI, Hill CP (2015). Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs). J Biol Chem, 290(21), 13490-9.
  5. The oligomeric state of the active Vps4 AAA ATPase.Monroe N, Han H, Gonciarz MD, Eckert DM, Karren MA, Whitby FG, Sundquist WI, Hill CP (2014). The oligomeric state of the active Vps4 AAA ATPase. J Mol Biol, 426(3), 510-25.
  6. Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler.Schubert HL, Wittmeyer J, Kasten MM, Hinata K, Rawling DC, Heroux A, Cairns BR, Hill CP (2013). Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. Proc Natl Acad Sci U S A, 110(9), 3345-50.
  7. Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill CP (2013). Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT. J Biol Chem, 288(15), 10188-94.
  8. Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function.Stadtmueller BM, Kish-Trier E, Ferrell K, Petersen CN, Robinson H, Myszka DG, Eckert DM, Formosa T, Hill CP (2012). Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function. J Biol Chem, 287(44), 37371-82.
  9. Structure and function of the membrane deformation AAA ATPase Vps4.Hill CP, Babst M (2012). Structure and function of the membrane deformation AAA ATPase Vps4. Biochim Biophys Acta, 1823(1), 172-81.
  10. Structure of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding.Zhai Q, Landesman MB, Robinson H, Sundquist WI, Hill CP (2011). Structure of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding. PLoS One, 6(12), e27466.
  11. An asymmetric interface between the regulatory and core particles of the proteasome.Tian G, Park S, Lee MJ, Huck B, McAllister F, Hill CP, Gygi SP, Finley D (2011). An asymmetric interface between the regulatory and core particles of the proteasome. Nat Struct Mol Biol, 18(11), 1259-67.
  12. Zhang H, Constantine R, Vorobiev S, Chen Y, Seetharaman J, Huang YJ, Xiao R, Montelione GT, Gerstner CD, Davis MW, Inana G, Whitby FG, Jorgensen EM, Hill CP, Tong L, Baehr W (2011). UNC119 is required for G protein trafficking in sensory neurons. Nat Neurosci, 14(7), 874-80.
  13. Activation of the retroviral budding factor ALIX.Zhai Q, Landesman MB, Chung HY, Dierkers A, Jeffries CM, Trewhella J, Hill CP, Sundquist WI (2011). Activation of the retroviral budding factor ALIX. J Virol, 85(17), 9222-6.
  14. Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain.Close D, Johnson SJ, Sdano MA, McDonald SM, Robinson H, Formosa T, Hill CP (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. J Mol Biol, 408(4), 697-713.
  15. Identification and structural characterization of the ALIX-binding late domains of simian immunodeficiency virus SIVmac239 and SIVagmTan-1.Zhai Q, Landesman MB, Robinson H, Sundquist WI, Hill CP (2011). Identification and structural characterization of the ALIX-binding late domains of simian immunodeficiency virus SIVmac239 and SIVagmTan-1. J Virol, 85(1), 632-7.
  16. Proteasome activators.Stadtmueller BM, Hill CP (2011). Proteasome activators. Mol Cell, 41(1), 8-19.

Review

  1. Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.LID - S0022-2836(15)00626-9 [pii]LID - 10.1016/j.jmb.2015.11.004 [doi]Monroe N, Hill CP (2015). Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.LID - S0022-2836(15)00626-9 [pii]LID - 10.1016/j.jmb.2015.11.004 [doi]. [Review]. J Mol Biol.
  2. Building a super elongation complex for HIV.Hill CP, Sundquist WI (2013). Building a super elongation complex for HIV. [Review]. eLife, 2, e00577.
  3. Structural biology of the proteasome.Kish-Trier E, Hill CP (2013). Structural biology of the proteasome. [Review]. Annual Review of Biophysics, 42, 29-49.

Editorial

  1. Editorial overview: Macromolecular machines and assemblies: Rise and fall at the molecular level.Forest KT, Hill CP (2015). Editorial overview: Macromolecular machines and assemblies: Rise and fall at the molecular level. Curr Opin Struct Biol, 31, vii-viii.