Skip to main content
Sign In

Resources For: Prospective Students | Current Students | Parents | Faculty & Staff | Alumni & Friends | Patients

 

Ulli Bayer, Assistant Professor

Ph.D. (1996), Heinrich-Pette- Institut
 

 

 

Contact Info:

Molecular Biology
University of Colorado

Ulli Bayer, Ph.D.  Research One North
(RC1-North), Room 6105 Ulli.Bayer@ucdenver.edu Phone: 303-724-3610

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).

 

Illario, M., Cavallo, A. L., Bayer, K. U., Di Matola, Fenzi, G. Rossi, G., and Vitale, M. (2003) Calcium/calmodulin-dependent proteinkinase II binds to Raf-1 and modulates integrinstimulated Erk activation. J. Biol. Chem., 278, 45101-45108.

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.

Nori, A., Lin, P. J., Galassi, L., Visentini, F., Cassetti, A., Villa, A., Bayer, K. U. and Volpe, P. (2003) Targeting of aKAP to sarcoplamic reticulum and nuclei of skeletal muscle. Biochem. J. 370, 873-880.

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

Leonard, A. S., Bayer, K. U., Merrill, M., Shea, M. A., Schulman, H. and Hell, J.W. (2002) Regulation of CaMKII docking to NMDA receptors by calcium/calmodulin and a-actinin. J. Biol. Chem., 277, 48441-48448.

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., Löhler, J., Schulman, H. and Harbers, K. (1999) Developmental expression of the CaM kinase II isoforms: ubiquitous g- and d-CaM kinase II are the early isoforms and most abundant in the developing nervous system. Mol. Brain Res., 70, 147-154.

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 brainspecifically expressed Ca2+/calmodulin-dependent kinase II a isoform gene in skeletal muscle. Mol. Cell. Biol., 16, 29-36.

Hamann, L., Bayer, K.-U., Jensen, K. and Harbers, K. (1994) Interaction of several related GC-box- and GT-box-binding proteins with the intronic enhancer is required for differential expression of the gb110 gene in embryonal carcinoma cells. Mol. Cell. Biol., 14, 5786-5793.