Photo of Greg Odorizzi

Greg Odorizzi

Professor
303.735.0179
Charles.Odorizzi@Colorado.EDU
Gold room A420C
Visit the Odorizzi Lab website.
Explore Greg Odorizzi's areas of research and more in Vivo
ORCID

Education

Ph.D., University of California, San Diego, 1996

Biography

Research Interests:
Cell biology and genetics of membrane trafficking and protein degradation

Research Profile:
Molecular contents are exchanged between organelles by the formation of membrane-enclosed vesicles that bud from one organelle and fuse with another. In principle, this process seems a simple one, yet it features many layers of regulation, with both protein and lipid components involved.

My lab investigates the molecular mechanisms of membrane trafficking from endosomes to lysosomes, which have a major role in protein degradation. Transmembrane proteins ubiquitinated on their cytoplasmic domains are sorted into vesicles that bud into the lumen of endosomes, resulting in their degradation upon fusion of endosomes with lysosomes. Molecular recognition of ubiquitinated transmembrane proteins requires an elaborate machinery known as the endosomal sorting complexes required for transport (ESCRTs). The ESCRT machinery is highly conserved throughout eukaryotes, and defects in its function make profound contributions to human disease.

The ESCRTs also have a role in the budding of transport vesicles that carry transmembrane proteins into the endosome lumen. Remarkably, this activity operates during cytokinesis to 'pinch' dividing cells apart, and enveloped viruses such as HIV exploit the ESCRTs in order to pinch away the plasma membrane of infected cells.

Our research is currently focused on defining the activities of ESCRTs that execute membrane budding reactions. Our model system is the yeast Saccharomyces cerevisiae, which enables us to combine genetics with cell biology, biochemistry, and electron tomographic modeling of membrane structures.

Selected Publications

Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies.
Richter, C, West, M, and Odorizzi, G EMBO J, 26(10):2454-64. 2007

Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway.
McNatt, MW, McKittrick, I, West, M, and Odorizzi, G Mol Biol Cell, 18(2):697-706. 2007

Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes.
Nickerson, DP, West, M, and Odorizzi, G J Cell Biol, 175(5):715-20. 2006

Molecular mechanisms of late endosome morphology, identity and sorting.
Russell, MRG, Nickerson, DP, and Odorizzi, G Curr Opin Cell Biol, 18(4):422-8. 2006

Structural basis for endosomal targeting by the Bro1 domain.
Kim, J, Sitaraman, S, Hierro, A, Beach, BM, Odorizzi, G, and Hurley, JH Dev Cell, 8(6):937-47. 2005