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.
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/
- PhD University of Massachusetts Medical Center
- Postdoctoral training: Yale University School of Medicine