TGF-alpha is synthesized as a transmembrane form (TM TGF-alpha) in most epithelial cells and can bind to the EGF/TGF-alpha receptor similar to its soluble form. However, the regulatory mechanisms that lead to the presentation and function of TM TGF- alpha are not clear yet. This application aims at the molecular and functional characterization of two TM TGF-alpha-associated proteins.
Aim 1 is aimed at characterizing the role of p59, which shows structural similarity to the Golgi protein GRASP 65. I will define the structural requirements of its interaction with TM TGF-alpha and characterize the potential roles of p59 on the intracellular routing, surface presentation of TM TGF-alpha, and on the cytoskeletal organization. I will give particular attention on how this association affects polarized transport of TM TGF-alpha in polarized epithelial cells.
Aim 2 should result in the isolation and characterization of another TM TGF-alpha- associated protein p86. The structural and functional characterization of the association of p86 with TM TGF-alpha will be studied in similar ways as for p59. These findings, in general, should contribute to an further understanding of how TGF-alpha and related growth factors affect the behavior and physiology of normal and tumor cells.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM020173-01
Application #
6013491
Study Section
Biological Sciences 2 (BIOL)
Program Officer
Lohrey, Nancy
Project Start
1999-07-01
Project End
Budget Start
1999-07-01
Budget End
2000-06-30
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost
Name
University of California San Francisco
Department
Dentistry
Type
Schools of Dentistry
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143