OHSU

William Skach, M.D.

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Background

Research Interests

  • Biogenesis of polytopic integral membrane proteins
  • Mechanisms of protein translocation and assembly in the endoplasmic reticulum
  • ER quality control and ER-associated degradation (ERAD)
  • Extraction and Degradation of polytopic membrane proteins
  • Current Projects

  • Molecular pathogenesis of cystic fibrosis.
  • Aquaporin biogenesis and transmembrane assembly.
  • Sec61 translocon function

  • Summary of Current Research

    Professor of Biochemistry & Molecular Biology Dr. Skach received his BS in Biochemistry and Biophysics from Oregon State University in 1979 and his MD Degree from Harvard Medical School in 1983. He completed clinical training in Internal Medicine, Hematology and Oncology at University of California, San Francisco and then undertook postdoctoral studies with Vishwanath Lingappa, also at UCSF. He started his laboratory at the University of Pennsylvania and moved to OHSU in 1998.


    Selected Publications

    "Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase," Journal of Biological Chemistry (Vol: 288, Issue: 43, Page 31069-31079) - 2013

    "Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate," Journal of Biological Chemistry (Vol: 287, Issue: 4, Page 2568-2578) - 2012

    "Thermal instability of Δf508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: Protection by single suppressor mutations and inhibiting channel activity," Biochemistry (Vol: 51, Issue: 25, Page 5113-5124) - 2012

    "Two-step insertion at the SecY translocon," Nature Structural and Molecular Biology (Vol: 19, Issue: 10, Page 975-977) - 2012

    "CFTR Folding Consortium: methods available for studies of CFTR folding and correction.," Methods in molecular biology (Clifton, N.J.) (Vol: 742, Page 335-353) - 2011

     

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    Contact

      Email William Skach

    503 494-7315