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Dr. Dieter Klopfenstein

Address
Dr. Dieter Klopfenstein
Drittes Physikalisches Institut
Abtl. Biophysik
Friedrich-Hund-Platz 1
37077 Göttingen
Tel.: +49-(0)551-39 13209
Fax: +49-(0)551-39 13208
e-mail: dklopfe@gwdg.de

GGNB Teaching
(Göttinger Graduiertenschule für Neurowissenschaften und Molekulare Biowissenschaften)
Molecular Biology (IMPRS)
Biomolecules: Structure - Function - Dynamics (GZMB)
Molecular Biology of Microbial, Animal and Plant Cells (GZMB)
Molecular Physiology of the Brain (CMPB)

C. Elegans                     MT kinesin model

The long-range transport of membrane organelles in neurons depends primarily upon microtubules and motor proteins that move unidirectionally along these tracks. One type of microtubule-based motor proteins powering membrane transport is the kinesin superfamily. We are interested in how these motors achieve specificity in cargo binding, elicit membrane transport, and the regulation of transport activity. One example of a kinesin motor is UNC-104/KIF1A, which specifically transports presynaptic vesicle to the synaptic terminal and binds with its tail domain directly to membrane lipids in vitro. This unique cargo-interaction mechanism help us to understand how lipids and their membrane environment contribute to cargo transport, how motor-lipid interaction could be regulating transport, and how accessory proteins contribute to membrane motility. Using fluorescently tagged motor and vesicle markers we investigate these questions in the nervous system of the nematode C. elegans serves us as a model system for microscopic tools (confocal, TIRF, FRET FLIM) and biochemical transport assays in vitro.


Biochemistry Teaching
http://www.uni-bc.gwdg.de/index.php


Selected Recent Publications
- Wagner OI, Esposito A, Köhler B, Chen CW, Shen CP, Wu GH, Mandalapu S, Wenzel D, Wouters FS, Klopfenstein DR (2009) Synaptic scaffolding protein SYD-2 clusters and activatesKinesin-3 UNC-104 in C. elegans. Proc Natl Acad Sci USA (PNAS Early Edition Week 44

- Klopfenstein DR, Vale RD (2004) The Lipid Binding Pleckstrin Homology Domain in UNC-104 Kinesin is Necessary for Synaptic Vesicle Transport in Caenorhabditis elegans. Mol Biol Cell 15(8):3729-39

- Al-Bassam J, Cui Y, Klopfenstein D, Carragher BO, Vale RD, Milligan RA (2003) Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition. J Cell Biol 163(4):743-53

- Tomishige M, Klopfenstein DR, Vale RD (2002) Dimerization triggers fast, processive movement of single Unc104/KIF1A kinesin motor along microtubules. Science 297(5590):2263-2267

- Klopfenstein DR, Tomishige M, Stuurman N, Vale RD (2002) Role of Phosphatidylinositol(4,5)bisphosphate Organization in Membrane Transport by the Unc104 Kinesin Motor. Cell 109(3):347-58

- Klopfenstein DR, Vale RD, Rogers SL (2000) Motor protein receptors: Moonlighting on other jobs. Cell 103(4):537-40