The regulated sorting of plasma membrane proteins is controlled by extracellular signals. A number of membrane proteins are retained intracellularly until their transport to the plasma membrane is stimulated by a particular signal. The transport of the S. cerevisiae general amino acid permease Gaplp is regulated in this manner. Under nutrient-limiting conditions, Gaplp is transported to the plasma membrane where it has high activity. Conversely, growth in nutrient-rich conditions results in little Gaplp at the plasma membrane, and low permease activity. Recently, a novel complex containing two small GTP-binding proteins has been shown to be required for Gaplp plasma membrane localization and activity (Gao and Kaiser, manuscript in preparation).
My aims are to: (1) Determine the intrinsic and activated guanine nucleotide binding and enzymatic properties of the GTPases, (2) Identify additional components of this Gaplp-sorting complex using biochemical and genomic means, and (3) Reconstitute the endosome-to-Golgi transport of Gaplp in vitro using purified membrane fractions and components, with the goal of identifying the requirements for this process. ? ?

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32GM075584-02
Application #
7123889
Study Section
Special Emphasis Panel (ZRG1-F05 (20))
Program Officer
Rodewald, Richard D
Project Start
2005-09-01
Project End
2008-08-31
Budget Start
2006-09-01
Budget End
2007-08-31
Support Year
2
Fiscal Year
2006
Total Cost
$48,796
Indirect Cost
Name
Massachusetts Institute of Technology
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
001425594
City
Cambridge
State
MA
Country
United States
Zip Code
02139