Chris A. Kaiser

Chris A. Kaiser

Professor of Biology; MacVicar Faculty Fellow

Chris A. Kaiser analyzes protein folding and trafficking in cells.

617-253-9804

Phone

68-340

Office

Gina Lee

Assistant

617-258-6473

Assistant Phone

Education

PhD 1987, Massachusetts Institute of Technology

Research Summary

We study protein folding and intracellular trafficking in the yeast S. cerevisiae. Our work focuses on the protein folding in the endoplasmic reticulum (ER), quality control mechanisms in the ER, and membrane protein sorting in Golgi compartments. We combine genetic, biochemical and cell biological methods to gain an understanding of the molecular mechanisms underlying each of these processes.

Recent Publications

  1. Balanced Ero1 activation and inactivation establishes ER redox homeostasis. Kim, S, Sideris, DP, Sevier, CS, Kaiser, CA. 2012. J. Cell Biol. 196, 713-25.
    doi: 10.1083/jcb.201110090PMID:22412017
  2. Transport activity-dependent intracellular sorting of the yeast general amino acid permease. Cain, NE, Kaiser, CA. 2011. Mol. Biol. Cell 22, 1919-29.
    doi: 10.1091/mbc.E10-10-0800PMID:21471002
  3. Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking. Risinger, AL, Kaiser, CA. 2008. Mol. Biol. Cell 19, 2962-72.
    doi: 10.1091/mbc.e07-06-0627PMID:18434603
  4. Ero1 and redox homeostasis in the endoplasmic reticulum. Sevier, CS, Kaiser, CA. 2008. Biochim. Biophys. Acta 1783, 549-56.
    doi: 10.1016/j.bbamcr.2007.12.011PMID:18191641
  5. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Sevier, CS, Qu, H, Heldman, N, Gross, E, Fass, D, Kaiser, CA. 2007. Cell 129, 333-44.
    doi: 10.1016/j.cell.2007.02.039PMID:17448992
  6. Activity-dependent reversible inactivation of the general amino acid permease. Risinger, AL, Cain, NE, Chen, EJ, Kaiser, CA. 2006. Mol. Biol. Cell 17, 4411-9.
    doi: 10.1091/mbc.e06-06-0506PMID:16885415
  7. Conservation and diversity of the cellular disulfide bond formation pathways. Sevier, CS, Kaiser, CA. Antioxid. Redox Signal. 8, 797-811.
    doi: 10.1089/ars.2006.8.797PMID:16771671
  8. A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast. Gao, M, Kaiser, CA. 2006. Nat. Cell Biol. 8, 657-67.
    doi: 10.1038/ncb1419PMID:16732272
  9. Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway. Rubio-Texeira, M, Kaiser, CA. 2006. Mol. Biol. Cell 17, 3031-50.
    doi: 10.1091/mbc.e05-07-0669PMID:16641373
  10. Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Sevier, CS, Kaiser, CA. 2006. Mol. Biol. Cell 17, 2256-66.
    doi: 10.1091/mbc.e05-05-0417PMID:16495342
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