TY - JOUR
T1 - Putative protein partners for the human CPI-17 protein revealed by bacterial two-hybrid screening
AU - Kim, Kyung mi
AU - Adyshev, Djanybek M.
AU - Kása, Anita
AU - Zemskov, Evgeny Alexandrovich
AU - Kolosova, Irina A.
AU - Csortos, Csilla
AU - Verin, Alexander D.
N1 - Funding Information:
This work was supported by NIH grants HL 58064 , HL 67307 , and HL101902 (for ADV), ALA Research Grant for Maryland (for IK), GHSU CVDI and AHA 11SDG7670035 grants (for EAZ), and the UD Faculty of Medicine Research Fund (Bridging Fund 2012) (for CsCs). The authors wish to thank Aigerim Adysheva for the technical assistance in the preparation of the manuscript.
PY - 2013/7
Y1 - 2013/7
N2 - We have previously demonstrated that PKC-potentiated inhibitory protein of protein phosphatase-1 (CPI-17) is expressed in lung endothelium. CPI-17, a specific inhibitor of myosin light chain phosphatase (MLCP), is involved in the endothelial cytoskeletal and barrier regulation. In this paper, we report the identification of fourteen putative CPI-17 interacting proteins in the lung using BacterioMatch Two-Hybrid System. Five of them: plectin 1 isoform 1, alpha II spectrin, OK/SW-CL.16, gelsolin isoform a, and junction plakoglobin are involved in actin cytoskeleton organization and cell adhesion, suggesting possible significance of these binding partners in CPI-17-mediated cytoskeletal reorganization of endothelial cells. Furthermore, we confirmed the specific interaction between plakoglobin and CPI-17, which is affected by the phosphorylation status of CPI-17 in human lung microvascular endothelial cells.
AB - We have previously demonstrated that PKC-potentiated inhibitory protein of protein phosphatase-1 (CPI-17) is expressed in lung endothelium. CPI-17, a specific inhibitor of myosin light chain phosphatase (MLCP), is involved in the endothelial cytoskeletal and barrier regulation. In this paper, we report the identification of fourteen putative CPI-17 interacting proteins in the lung using BacterioMatch Two-Hybrid System. Five of them: plectin 1 isoform 1, alpha II spectrin, OK/SW-CL.16, gelsolin isoform a, and junction plakoglobin are involved in actin cytoskeleton organization and cell adhesion, suggesting possible significance of these binding partners in CPI-17-mediated cytoskeletal reorganization of endothelial cells. Furthermore, we confirmed the specific interaction between plakoglobin and CPI-17, which is affected by the phosphorylation status of CPI-17 in human lung microvascular endothelial cells.
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U2 - 10.1016/j.mvr.2013.04.002
DO - 10.1016/j.mvr.2013.04.002
M3 - Article
C2 - 23583905
AN - SCOPUS:84878561498
SN - 0026-2862
VL - 88
SP - 19
EP - 24
JO - Microvascular Research
JF - Microvascular Research
ER -