Project Details
Projekt
The role of ubiquitination in the transport and turnover of membrane proteins
Applicant
Professor Dr. Ralf Kölling, since 10/2004
Subject Area
Biochemistry
Term
from 2000 to 2005
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 5249322
Many cell surface proteins are modified by ubiquitination. Recent experiments indicate that this ubiquitination is not tied to the action of the proteasome. Instead, ubiquitination appears to be used as a signal for endocytosis and vacuolar targeting of these membrane proteins. However, many questions concerning the role of ubiquitination in the trafficking of membrane proteins are still unresolved. We are studying the role of ubiquitination in the intracellular transport and turnover of the yeast a-factor transporter Ste6. To define the role of ubiquitination in Ste6 trafficking, we will examine the consequences of a loss in Ste6 ubiquitination. Ubiquitination will be eliminated by inactivation of the ubiquitin attachment site(s) and by interfering with the ubiquitin machinery which attaches ubiquitin onto Ste6. The effects of these manipulations on the half-life and the intracellular distribution of Ste6 will be examined.
DFG Programme
Priority Programmes
