Project Details
Projekt
FOR 885: Neuronal Protein Turnover
Subject Area
Medicine
Term
from 2007 to 2013
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 35615435
Basic mechanisms of protein turnover include the ubiquitin/proteasome system, targeting of membrane proteins to the endosomal/lysosomal pathway, as well as autophagosome and aggresome formation. In recent years these mechanisms have been elucidated in molecular detail, mostly in non-neuronal cells. However, it is unclear how these degradative systems work in neurons. Neurons have special requirements for synthetic and degradative pathways, as they are polarised and extend cellular processes over long distances. The majority of proteins are synthesised in the soma of neurons, but exert their function in distant processes. Thus, local control of protein turnover is required for the maintenance of excitability, synaptic transmission and synaptic plasticity, important characteristics of the nervous system.
The main goal of the Research Unit is to understand how neurons employ mechanisms of protein turnover to fulfill specific neuronal functions. Therefore, we will address the following questions:
(1) Which components are involved in neuron specific protein degradation?
(2) How does neuronal protein turnover contribute to the regulation of neuronal excitability and synaptic plasticity?
(3) How does impaired neuronal protein trafficking influence the functionality of neurons?
In order to address these questions scientists with diverse scientific backgrounds in basic medical research, theoretical medical disciplines and molecular neurobiology have joined forces. A variety of biological systems and technical approaches will be used to solve these questions, including genetic screens in C. elegans, transgenic and knock-out mouse models and cellular imaging techniques within the context of primary cultured neurons.
The main goal of the Research Unit is to understand how neurons employ mechanisms of protein turnover to fulfill specific neuronal functions. Therefore, we will address the following questions:
(1) Which components are involved in neuron specific protein degradation?
(2) How does neuronal protein turnover contribute to the regulation of neuronal excitability and synaptic plasticity?
(3) How does impaired neuronal protein trafficking influence the functionality of neurons?
In order to address these questions scientists with diverse scientific backgrounds in basic medical research, theoretical medical disciplines and molecular neurobiology have joined forces. A variety of biological systems and technical approaches will be used to solve these questions, including genetic screens in C. elegans, transgenic and knock-out mouse models and cellular imaging techniques within the context of primary cultured neurons.
DFG Programme
Research Units
Projects
- Central administrative tasks, seminars, travel and publication costs (Applicant Glatzel, Markus )
- IRP3: KCNQ (Kv7) channel turnover and cellular excitability (Applicant Pongs, Olaf )
- IRP5: FIX proteins as regulators of receptor tyrosine kinase endocytosis and actin dynamics (Applicant Kutsche, Kerstin )
- RP1: Identification of ubiquitin-dependent pathways involved in neuron-specific protein degradation (Applicant Hoppe, Thorsten )
- RP4: Synaptic regulation of GABAA receptor turnover (Applicant Kneussel, Ph.D., Matthias )
- RP6: Degradative routes of intracellular proteins in lysosomal disorders (Applicant Braulke, Thomas )
- RP7: Investigation of novel mechanisms in degradation of aggregated neuroserpin (Applicants Glatzel, Markus ; Hoppe, Thorsten )
- RP8: The neuronal interactome of mitochondrial m-AAA proteases (Applicant Langer, Thomas )
- RP9: Ubiquitylation-controlled Arc/Arg3.1 translation and protein turnover in synaptic plasticity and memory consolidation (Applicant Kuhl, Dietmar )
- RP10: Role of Parkin in regulating GDNF signal transduction and receptor turnover in neurons (Applicant Kramer, Edgar Richard )
- Ubiquitylation and degradation of postsynaptic scaffold proteins (Applicant Kreienkamp, Hans-Jürgen )
Spokesperson
Professor Dr. Markus Glatzel
