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Investigating Myosin Light Chain Kinase Binding with Actin in Human Airway Smooth Muscle Cells
Date
2015Type
ThesisDepartment
Biochemistry and Molecular Biology
Degree Level
Honors Thesis
Degree Name
Biochem and Molecular Biology
Abstract
Myosin light chain kinase plays an integral role in initiating and regulating
smooth muscle contraction. These experiments were conducted to help illuminate and
better understand the process by which myosin light chain kinase interacts with actin and
myosin in the ventral stress fibers of permeabilized human airway smooth muscle cells.
The first 75 residues of the N-terminal end of MLCK (GST tagged N75) contain the three
DFRXXL motifs, which are sufficient for actin binding [1-4]. N75 binding to actin was
imaged using fluorescence microscopy and total internal reflection microscopy under
varying conditions. N75 binding was inhibited when cells were pre-treated with the S1
fragment of myosin heads. This suggests that the DFRXXL motifs of MLCK are
competing with S1 for actin binding sites. These experiments help better the
understanding of the role myosin light chain kinase plays in the regulation and
contraction of smooth muscle contraction.
Permanent link
http://hdl.handle.net/11714/642Additional Information
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