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Department of Pharmacology

Department of Pharmacology
 

Ulli Bayer, PhD

Associate Professor


Contact Information:

University of Colorado Denver
Department of Pharmacology
Mail Stop 8303, RC1-North
12800 East 19th Ave
Aurora CO 80045

Phone: (303) 724-3610
Fax: (303) 724-3663
E-mail: ulli.bayer@ucdenver.edu
curriculum vitae

Affiliated Programs

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My laboratory is interested in mechanisms of molecular memory and their use in cellular signal transduction and neuronal function. In the nervous system, we want to know how the ability of proteins to "remember" past molecular events is implemented in synaptic plasticity underlying the ability of our brains to learn and retain memories. CaMKII, a Ca2+ activated protein kinase highly enriched in brain, is an ideal model protein for the investigation of these questions. Ca2+ and CaMKII are required in several forms of synaptic plasticity and learning, and CaMKII displays several interesting forms of molecular memory. Molecular memory enables CaMKII to integrate Ca2+ signals over time and to act as molecular decoder of Ca2+ spike frequencies. Our primary goal is to better understand the mechanisms underlying neuronal plasticity and learning, but our research also has direct implication for stroke and neurodegenerative diseases.

Ca2+ signaling has important functions also outside the nervous system, including heart function, muscle contraction, and insulin secretion. My lab is also interested in how these functions are regulated by CaMKII; some of the cellular mechanisms may be similar to those used by neurons. Frequency decoding, for instance, makes CaMKII an ideal candidate for a molecular heart rate sensor, and roles of CaMKII in heart diseases such as dilated hypertrophy are emerging.

The tools we use in our research include molecular manipulations of neurons and other cells in tissue culture, live imaging of labeled proteins within cells, and biochemical analysis of purified proteins in vitro (including regulation of activity, protein-protein interactions, and modes of frequency detection).

Current Lab Members

 Results From Personnel : Selected site and subsites
First NameLast NameMiddle InitialDegreePosition
KelseyBarcombM.BAGraduate Student
StevenCoultrapJ.PhDSenior Research Associate
DaytonGoodell BSGraduate Student
NicholasHaynes BSProfessional Research Assistant

 

Previous Trainees

 Results From Personnel : Selected site and subsites
First NameLast NameMiddle InitialDegreePosition
IsabelleBuard PhDPostdoctoral Fellow
StevenCoultrapJ.PhDPostdoctoral Fellow
EricHorneA.PhDPostdoctoral Fellow
HeatherO'LearyE.PhDGraduate Student
RebekahVestS.PhDGraduate Student

 

 

View Dr. Bayer's Publications on PubMed

Selected Publications:  

Vest R. S., Davies K. D., O'Leary H., Port J. D., Bayer K. U. (2007) Dual mechanism of a natural CaMKII inhibitor. Mol Biol Cell., 18(12):5024-33.

O’Leary, H., Lasda, E. and Bayer, K. U. (2006) CaMKIIb association with the actin cytoskeleton is regulated by alternative splicing. Mol. Biol. Cell., 17:4646-4665.

Bayer, K. U., LeBel, E., McDonald, G. L., O’Leary, H., Schulman, H. and DeKoninck, P. (2006) Transition from reversible to persistant binding of CaMKII to postsynaptic sites and NR2B. J. Neurosci.. 26, 1164-1174.

Fink, C., Bayer, K. U., Myers, J. W., Ferrell, J. E. Schulman, H. and Meyer, T. (2003) Selective regulation of neurite extension, movement and branching by the b but not the a isoform of CaMKII. Neuron, 39, 283-297.

Bayer, K. U., De Koninck, P. and Schulman, H. (2002) Alternative splicing modulates the frequency-dependent response of CaMKII to Ca2+-oscillations. EMBO J., 21, 3590-3597.

Bayer, K.-U., De Koninck, P., Leonard, A.S., Hell, J.W. and Schulman, H. (2001) Interaction with the NMDA receptor locks CaMKII in an active conformation. Nature, 411, 801-805.

Bayer, K.-U., Harbers, K. and Schulman, H. (1998) aKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle. EMBO J., 17, 5598-5605.

Bayer, K.-U., Löhler, J. and Harbers, K. (1996) An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II a isoform gene in skeletal muscle. Mol. Cell. Biol., 16, 29-36.