Will Prinz : NIDDK

Will Prinz


LCBB
CELL BIOCHEMISTRY SECTION
NIDDK, National Institutes of Health
Building 8, Room 301
8 Center Dr.
Bethesda, MD 20892-0851
Tel: 301-451-4592
Fax: 301-496-9431
Email: wp53m@nih.gov

Education / Previous Training and Experience:
PhD. Harvard University, 1996


Research Statement:

My lab studies different aspects of organelle biogenesis in the model organism S. cerevisiae with a combination of biochemical, genetic, and imaging approaches. Here are three projects in the lab:

1. Intracellular lipid trafficking. Relatively little is known about how cells determine the lipid composition of organelles and regulate intracellular lipid transport. Numerous diseases, including heart disease and Type 2 diabetes, are associated with defects in these processes. The lipid composition of organelles is determined by both modulating the lipid composition of intracellular transport vesicles and nonvesicular lipid transport between organelles. Neither process is well understood. We are working to identify proteins required for nonvesicular lipid trafficking in cells and understand their role in organelle biogenesis and lipid metabolism. We have recently found that some members of a large family of lipid binding proteins known as oxysterol-binding proteins can transfer sterols such as cholesterol and ergosterol in cells. We are currently working to understand the regulation and functions of these proteins. Other projects focus on phospholipid trafficking to mitochondria and peroxisomes.

2. Proteins that determine ER structure. In yeast and higher eukaryotes, portions of the ER form a dynamic tubular network, often closely apposed to the plasma membrane. This structure is thought to be important for proper organelle function, but how it is established and maintained is not well understood. In collaboration with Gia Voeltz and Tom Rapoport at Harvard Medical School we have recently found a role for a large family of proteins known as reticulons in determining ER structure. We are working to understand how these proteins shape membranes and function in cells.

3. Calmodulin-dependent nuclear import. High mobility group (HMG) proteins are a large family of transcription factors that control many regulatory and developmental pathways in mammals. Nuclear import is a key step in the regulation in many of these proteins. Interestingly, many HMG proteins may be imported into the nuclear by a novel calmodulin-dependent nuclear import pathway. We study the yeast HMG protein Nhp6ap and have found that it also requires calmodulin, but not RAN, for nuclear import. We are working to identify other proteins required for this novel nuclear import pathway.



Selected Publications:

Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA  A class of membrane proteins shaping the tubular endoplasmic reticulum.  Cell (124): 573-86, 2006. [Full Text/Abstract]

Raychaudhuri S, Im YJ, Hurley JH, Prinz WA  Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides.  J Cell Biol (173): 107-19, 2006. [Full Text/Abstract]

Im YJ, Raychaudhuri S, Prinz WA, Hurley JH  Structural mechanism for sterol sensing and transport by OSBP-related proteins.  Nature (437): 154-8, 2005. [Full Text/Abstract]

Li Y, Prinz WA  ATP-binding cassette (ABC) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum.  J Biol Chem (279): 45226-34, 2004. [Full Text/Abstract]

Prinz W  Cholesterol trafficking in the secretory and endocytic systems.  Semin Cell Dev Biol (13): 197-203, 2002. [Full Text/Abstract]

Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, Rapoport TA  Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae.  J Cell Biol (150): 461-74, 2000. [Full Text/Abstract]



Page last updated: December 17, 2008

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