Wesley I. Sundquist, Ph.D.

Co-Chair, Department of Biochemistry

Research Interests

  • ESCRT Pathway
  • Protein Design
  • Cytokinesis
  • Immunity
  • HIV
  • Structural Biology of Retroviruses

Labs

Lab Website

Academic Information

  • Departments: Biochemistry - Professor
  • Cancer Center Programs: Cell Response & Regulation

Academic Office Information

  • (801) 585-5402
  • Emma Eccles Jones Research Building
    Department of Biochemistry
    15 North Medical Drive East, Room: 3532C
    Salt Lake City, UT 84112

Research Statement

The Sundquist Lab studies the cellular, molecular and structural biology of retroviruses, particularly HIV, and the roles of the ESCRT pathway in cell division and the abscission checkpioint. Major projects in our lab include studies of: 1) ESCRT pathway functions and regulation in cell division, 2) HIV budding, and 3) HIV capsid structure, function and restriction, particularly by the TRIM5α system. Our approaches include NMR, EM, crystallographic and compuational studies of viral complexes, identification and biochemical analyses of the interactions between viral components and their cellular partners, and genetic analyses of viral and cellular protein functions.

Academic Bio

Wesley Sundquist, PhD, is Samuels Professor and Co-Chair of the Department of Biochemistry at the University of Utah. He is also a member of the Cell Response and Regulation Program at Huntsman Cancer Institute.

Sundquist received a bachelor's degree from Carleton College, Minnesota, and a PhD from the Massachusetts Institute of Technology. His honors and awards include election to the American Academy of Arts and Sciences and the National Academy of Sciences

Education History

Type School Degree
Postdoctoral Fellowship MRC Laboratory of Molecular Biology
Biochemistry
Postdoctoral Fellow
Doctoral Training Massachusetts Institute of Technology
Chemistry
Ph.D.
Undergraduate Carleton College
Chemistry
B.A.

Global Impact

Education History

Type School Degree Country
Postdoctoral Fellowship MRC Laboratory of Molecular Biology
Biochemistry
Postdoctoral Fellow United Kingdom

Career

Institution Description Country
Structural Studies Division, MRC Laboratory of Molecular Biology Postdoctoral Fellow United Kingdom

Selected Publications

Journal Article

  1. Votteler J, Ogohara C, Yi S, Hsia Y, Natterman U, Belnap DM, King NP, Sundquist WI (2016 Dec 8). Designed proteins induce the formation of nanocage-containing extracellular vesicles. Nature, 540(7632), 292-295.
  2. Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5alpha.LID - 10.7554/eLife.16309 [doi]LID - e16309 [pii]Wagner JM, Roganowicz MD, Skorupka K, Alam SL, Christensen D, Doss G, Wan Y, Frank GA, Ganser-Pornillos BK, Sundquist WI, Pornillos O (2016). Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5alpha.LID - 10.7554/eLife.16309 [doi]LID - e16309 [pii]. Elife, 5.
  3. Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.LID - 10.7554/eLife.16269 [doi]LID - e16269 [pii]Li YL, Chandrasekaran V, Carter SD, Woodward CL, Christensen DE, Dryden KA, Pornillos O, Yeager M, Ganser-Pornillos BK, Jensen GJ, Sundquist WI (2016). Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.LID - 10.7554/eLife.16269 [doi]LID - e16269 [pii]. Elife, 5.
  4. Structure and membrane remodeling activity of ESCRT-III helical polymers.McCullough J, Clippinger AK, Talledge N, Skowyra ML, Saunders MG, Naismith TV, Colf LA, Afonine P, Arthur C, Sundquist WI, Hanson PI, Frost A (2015). Structure and membrane remodeling activity of ESCRT-III helical polymers. Science, 350(6267), 1548-51.
  5. Angiomotin functions in HIV-1 assembly and budding.LID - 10.7554/eLife.03778 [doi]Mercenne G, Alam SL, Arii J, Lalonde MS, Sundquist WI (2015). Angiomotin functions in HIV-1 assembly and budding.LID - 10.7554/eLife.03778 [doi]. Elife, 4.
  6. 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.
  7. ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins.Caballe A, Wenzel DM, Agromayor M, Alam SL, Skalicky JJ, Kloc M, Carlton JG, Labrador L, Sundquist WI, Martin-Serrano J (2015). ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins. Elife, 4, e06547.
  8. TRIM5alpha requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription.Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ (2015). TRIM5alpha requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription. EMBO J, 34(15), 2078-95.
  9. The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.Sanchez JG, Okreglicka K, Chandrasekaran V, Welker JM, Sundquist WI, Pornillos O (2014). The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer. Proc Natl Acad Sci U S A, 111(7), 2494-9.
  10. 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.
  11. ESCRT requirements for EIAV budding.Sandrin V, Sundquist WI (2013). ESCRT requirements for EIAV budding. Retrovirology, 10(1), 104.
  12. ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding.Effantin G, Dordor A, Sandrin V, Martinelli N, Sundquist WI, Schoehn G, Weissenhorn W (2013). ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell Microbiol, 15(2), 213-26.
  13. Discovery of novel small-molecule HIV-1 replication inhibitors that stabilize capsid complexes.Lamorte L, Titolo S, Lemke CT, Goudreau N, Mercier JF, Wardrop E, Shah VB, von Schwedler UK, Langelier C, Banik SS, Aiken C, Sundquist WI, Mason SW (2013). Discovery of novel small-molecule HIV-1 replication inhibitors that stabilize capsid complexes. Antimicrob Agents Chemother, 57(10), 4622-31.
  14. Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport.Skalicky JJ, Arii J, Wenzel DM, Stubblefield WM, Katsuyama A, Uter NT, Bajorek M, Myszka DG, Sundquist WI (2012). Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport. J Biol Chem, 287(52), 43910-26.
  15. ALIX is a Lys63-specific polyubiquitin binding protein that functions in retrovirus budding.Dowlatshahi DP, Sandrin V, Vivona S, Shaler TA, Kaiser SE, Melandri F, Sundquist WI, Kopito RR (2012). ALIX is a Lys63-specific polyubiquitin binding protein that functions in retrovirus budding. Dev Cell, 23(6), 1247-54.
  16. Distinct effects of two HIV-1 capsid assembly inhibitor families that bind the same site within the N-terminal domain of the viral CA protein.Lemke CT, Titolo S, von Schwedler U, Goudreau N, Mercier JF, Wardrop E, Faucher AM, Coulombe R, Banik SS, Fader L, Gagnon A, Kawai SH, Rancourt J, Tremblay M, Yoakim C, Simoneau B, Archambault J, Sundquist WI, Mason SW (2012). Distinct effects of two HIV-1 capsid assembly inhibitor families that bind the same site within the N-terminal domain of the viral CA protein. J Virol, 86(12), 6643-55.
  17. Global landscape of HIV-human protein complexes.Jager S, Cimermancic P, Gulbahce N, Johnson JR, McGovern KE, Clarke SC, Shales M, Mercenne G, Pache L, Li K, Hernandez H, Jang GM, Roth SL, Akiva E, Marlett J, Stephens M, DOrso I, Fernandes J, Fahey M, Mahon C, ODonoghue AJ, Todorovic A, Morris JH, Maltby DA, Alber T, Cagney G, Bushman FD, Young JA, Chanda SK, Sundquist WI, Kortemme T, Hernandez RD, Craik CS, Burlingame A, Sali A, Frankel AD, Krogan NJ (2011). Global landscape of HIV-human protein complexes. Nature, 481(7381), 365-70.

Commentary

  1. McCullough J, Sundquist WI (2014). Putting a finger in the ring. Nat Struct Biol, 21(12), 1025–1027.

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