Christine Cremo

Photo of Christine Cremo


Department of School of Medicine - UNR
University of Nevada/Mail Stop 330
1664 North Virginia Street, UNSOM
Reno,  Nevada   89557

Office: (775) 784-7033
Lab: 784-7032

Fax: 784-1419

Building: Howard Medical Science,  Office 153

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Diamond High School, Anchorage Alaska
B.A. Lewis & Clark College 1977
Ph.D. Oregon State University 1983


My laboratory is interested in the mechanisms that regulate contraction of smooth muscles. We use biophysical, structural, and kinetic techniques to study the structure and function of myosin and actin, the major contractile proteins. These studies are addressing the structural mechanisms that control the activity of myosin. Smooth muscle myosin is regulated by phosphorylation, resulting in large conformational changes. The inactive unphosphorylated state is self-inhibited by interaction of the myosin tail domain with the catalytic and regulatory domains. We are studying the structure of this inhibited state by photocross-linking, fluorescence quenching and polarization, electron paramagnetic resonance, phosphorescence anisotropy, mass spectrometry and crystallography. Self-inhibited myosin is in equilibrium with myosin filaments, which is the force-generating conformation.

We are interested in understanding the regulation of this equilibrium in the cell. Major approaches are measurements of contractile force in intact tissues, immunofluorescence microscopy of transiently-transfected cells, dynamic imaging of GFP- and other fluorescent constructs in live cells, mutagenesis, and fluorescence photo-bleaching recovery.


Medical Biochemistry 602


NIH grant in 17th year of continuous funding

Topographical Studies of Smooth and Nonmuscle Myosins

Co-PI for COBRE, Smooth Muscle Plasticity, University of Nevada School of Medicine


Member - American Heart Association Study Section (National Organization) - Cellular Cardiovascular Physiology and Pharmacology (1994-1997) 

Member - American Heart Association Study Section -Washington/Oregon Affiliate (1995-1997)

Invited Participant - Roundtable Discussion on Future of Muscle Biology at the National Institute of Arthritis and Musculoskeletal and Skin Diseases (Chaired by Dr. Stephen Katz, Director) (June 1996)

Member - Site Visit Team, Program Project Grant Review for Boston Biomedical Research Institute (NAIMS, The NIH) 1996

Co-Chair, Biophysical Society, Motility Subgroup (1997-98)

Co-chair, American Heart Association Study Section (National Organization) - Cellular Cardiovascular Physiology and Pharmacology (1997-8)

Co-chair, Great America Consortium Peer Review Committee, Cardiovascular Regulation, American Heart Association (1998-2000)

Member - American Heart Association Study Section, Molecular Biology of the Muscle (1999-2001)

Editorial Board Member, Journal of Biological Chemistry (2001-2006)

Member – National Institute of Arthritis and Musculoskeletal Disease, 2001 Site Visit Team, Program Project Grant Review for University of Vermont, Department of Molecular Physiology and Biophysics, College of Medicine, Myosin Dynamics during the Contractile Cycle

Member, National Heart Lung and Blood Institute (NHLBI), ad hoc reviewer (2000-2001).

Member, Special Study Section B, National Institutes of Health, 2001.

Bioinformatics Core Facility, University of Nevada, Reno; Advisory Board Member, Structural Bioinformatics (2002-2004)

Member, AHA Basic Cell Biology Study Section 1, 2002-2005

Ad hoc reviewer, Macromolecular Structure and Function C Study Section, National Institutes of Health, 2005

Member, AHA Basic Cell & Molecular Biology 1 Study Section 2006-present

Member, Editorial Board, Journal of Muscle Research and Cell Motility, 2006- present


Feng Hong, Brian D. Haldeman, Del Jackson, Mike Carter, Jonathan E. Baker, Christine R. Cremo 2011, Biochemistry of smooth muscle myosin light chain kinase, Archives of Biochemistry and Biophysics - vol. 510, no. 2, pp. 135-146

The smooth muscle isoform of myosin light chain kinase (MLCK) is a Ca2+-calmodulin-activated kinase that is found in many tissues. It is particularly important for regulating smooth muscle contraction by phosphorylation of myosin. This review summarizes selected aspects of recent biochemical work on MLCK that pertains to its function in smooth muscle. In general, the focus of the review is on new findings, unresolved issues, and areas with the potential for high physiological significance that need further study. The review includes a concise summary of the structure, substrates, and enzyme activity, followed by a discussion of the factors that may limit the effective activity of MLCK in the muscle. The interactions of each of the many domains of MLCK with the proteins of the contractile apparatus, and the multi-domain interactions of MLCK that may control its behaviors in the cell are summarized. Finally, new in vitro approaches to studying the mechanism of phosphorylation of myosin are introduced.

Hyun Suk Jung, Neil Billington, Kavitha Thirumurugan, Bridget Salzameda, Christine R. Cremo, Joseph M. Chalovich, Peter D. Chantler, Peter J. Knight 2011, Role of the Tail in the Regulated State of Myosin 2, Journal of Molecular Biology, vol. 408, no. 5, pp. 863-878
Cremo, C. R., Ba, M., Singer, C., Manoj, T., Brophy, C., Baker, J., Halayko, A., Gerthoffer, W. T. 2009, HSP20 phosphorylation and airway smooth muscle relaxation., Cell Health and Cytoskeleton, 1, 27-42.