The CDK5 activator, p39, binds specifically to myosin essential light chain
| Autor: | Peggy S. Zelenka, Brajendra K. Tripathi, Dolena R. Ledee |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Myosin Light Chains
Myosin light-chain kinase Immunoprecipitation Biophysics Nerve Tissue Proteins Biology Immunoglobulin light chain Biochemistry Article Two-Hybrid System Techniques Chlorocebus aethiops Lens Crystalline Myosin medicine Animals Binding site Cytoskeleton Molecular Biology Binding Sites COS cells Myosin Heavy Chains Cyclin-Dependent Kinase 5 Cell Biology Rats Cell biology medicine.anatomical_structure Lens (anatomy) COS Cells Rabbits Subcellular Fractions |
| Zdroj: | Biochemical and Biophysical Research Communications. 354:1034-1039 |
| ISSN: | 0006-291X |
| Popis: | Cyclin-dependent kinase 5 (Cdk5) has been shown to regulate adhesion and migration of lens and corneal epithelial cells. To explore protein–protein interactions that may mediate these functions, we performed yeast two-hybrid screening on an embryonic rat lens library using Cdk5 and its regulators, p35 and p39 as baits. This screen identified an interaction between p39 and non-muscle myosin essential light chain (MLC17). GST pull-down experiments demonstrated that p39 binds directly to MLC17 through a strong binding site in the N-terminal 109 amino acids of p39. Immunoprecipitation of proteins from Cos1 cells co-transfected with GFP–MLC17 and HA-p39 confirmed that these proteins interact intracellularly. Immunofluorescence microscopy of co-transfected lens epithelial cells showed that GFP–MLC17 and HA-p39 co-localize along cytoskeletal fibrils. Moreover, endogenous rat lens p39 co-immunoprecipitated with MLC17 and myosin heavy chain II (MHC II), demonstrating that the interaction is physiological and serves to link p39 to the cytoskeleton. |
| Databáze: | OpenAIRE |
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