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Daniel Hebert

Professor

We are interested in understanding the processes involved in the proper maturation and quality control of glycoproteins that traverse the mammalian secretory pathway, and how aberrant proteins are cleared.

Current Research
Cellular processes, including protein trafficking in the endoplasmic reticulum (ER), are controlled by molecular machines commonly found in large interconnected macromolecular complexes. The quality control process of the ER directs the flux of maturing proteins in the secretory pathway by determining whether to divert maturing proteins to macromolecular complexes involved in transport, ER retention or degradation. How these critical decisions are made, as well as the composition and inter-relatedness of many ER protein complexes is incompletely understood. Retention and subsequent degradation of ER-trafficked proteins, as dictated by the quality control processes, is the basis for a large number of human disease states including cystic fibrosis, liver cirrhosis, albinism and emphysema to name a few, because of the loss of key cellular activities. Protein maturation defects may result from disruptions in protein folding, signal sequence cleavage, glycosylation, oxidation or assembly. We are interested in understanding the maturation and quality control processes for a number of both soluble and membrane inserted glycoproteins. This involves mapping the molecular choreography for maturing nascent chains, as well as understanding the roles and mechanisms of action of the ER resident proteins that assist these folding, maturation, interrogation, sorting and trafficking processes.

Learn more at people.biochem.umass.edu/hebertlab/

Academic Background

  • PhD University of Massachusetts Medical Center
  • Postdoctoral training: Yale University School of Medicine
Tannous A., N. Patel, T. Tamura, and D. N. Hebert. (2015) Reglucosylation by UDP-glucose: glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation. Molecular Biology of the Cell, 26(3):390-405.
Tannous A., G. B. Pisoni, D. N. Hebert and M. Molinari. (2015) N-linked sugar regulated protein folding and quality control in the ER, Seminars in Cell and Developmental Biology, in press.
Hebert, D. N., L. Lamriben, E. T. Powers and J. W. Kelly. (2014) The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis. Nature Chemical Biology, 10(11):902-910.
Guiliano, D.B, H. Fussell, I. Lenart, E. Tsao, D. Nesbeth, A. Fletcher, E. C. Campbell, S. Lynch, S. Santos, A. Cameron, G. Towers, P. Kellam, D. N. Hebert, K. Gould, S. J. Powis, and A. N. Antoniou. (2014) HLA-B27 dimers preferentially interact with EDEM1 and are targeted for degradation by an HRD1-dependent pathway. Arthritis & Rheumatology, 66(11):2976-88.
Sunryd, J. C., T. Tannous, L. Lamriben and D. N. Hebert (2014) Chaperones of the ERAD pathway. In W. A. Houry (ed.), The Molecular Chaperones Interaction Networks in Protein Folding and Degradation, Springer Press.
Braakman, I. and D. N. Hebert (2013) “Protein folding in the endoplasmic reticulum”, in Ferro-Novick, S, R. Schekman, and T. Rapoport (ed.), Endoplasmic Reticulum Monograph, Cold Spring Harbor Laboratory Press. May 1;5(5):a013201.
Giorda KM, Hebert DN. (2013) Viroporins customize host cells for efficient viral propagation. DNA & Cell Biol. 2013 Oct;32(10):557-64.
Raghava, S., K. M. Giorda, F. B. Romano, A. P. Heuck and D. N. Hebert (2013) SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release. Biochemistry. 2013 Jun 4;52(22):3939-48.
Giorda, K. M., S. Raghava, M. W. Zhang and D. N. Hebert (2013) The viroporin activity of the minor structural proteins VP2 and VP3 is required for SV40 propagation. Journal of Biological Chemistry, 288(4):2510-2520.
 
Contact Info

Department of Biochemistry and Molecular Biology
N327 Life Sciences Laboratory
240 Thatcher Way
Amherst, MA 01003-9292

(413) 545-0079
dhebert@biochem.umass.edu

people.biochem.umass.edu/hebertlab/