Untersuchungen zur Rolle der Ubiquitinierung beim intrazellulären Transport und Turnover von Membranproteinen

• Antragsteller: Professor Dr. Ralf Kölling, seit 10/2004
• Fachliche Zuordnung: Biochemie
• Förderung: Förderung von 2000 bis 2005
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 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-Verfahren: Schwerpunktprogramme
• Teilprojekt zu: SPP 1045: Struktur, Funktion und Regulation des 20S/26S Ubiquitin-Proteasomsystems