COMMD6 from amphioxus Branchiostoma belcheri (BbCOMMD6) interacts with creatine kinase and inhibits its activity |
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| Authors: | Peipei Li Shicui Zhang Chunxin Fan |
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| Affiliation: | 5. From the Department of Biochemistry, Weill Cornell Medical College, New York, New York 10065,;3. the Institute of Biochemistry and Molecular Medicine, University of Bern, 3012 Bern, Switzerland,;4. the Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390,;6. the Department of Microbiology and Immunology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, New York 14214, and;1. Department of Hepatobiliary Pancreatic Surgery, China-Japan Union Hospital of Jilin University, Changchun, 130033, China;2. Department of Pharmacology and Toxicology, Wright State University, Fairborn, OH, 45435, USA;3. Department of Breast Surgery, China-Japan Union Hospital of Jilin University, Changchun, 130033, China;1. Division of Experimental Pathology, Institute of Pathology, University of Bern, Bern, Switzerland;2. Experimental Oncology/Hematology, Department of Clinical Research, University of Bern, Bern, Switzerland;3. Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland;4. Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA;5. Department of Medical Oncology, Inselspital, Bern University Hospital, Bern, Switzerland |
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| Abstract: | COMM domain-containing proteins are a group of recently discovered proteins; their biochemical characterization remains much limited. Here we demonstrate that a cDNA encoding Branchiostoma belcheri COMMD6, designated BbCOMMD6, codes for a protein of 203 amino acids, with a COMM domain at its C-terminal region and an extended N-terminal portion. BbCOMMD6 is mainly present in the cytosol. In contrast to COMMD1, the presence of Cu(II) cannot enhance recombinant BbCOMMD6 dimer formation. Both the pull-down and reverse pull-down assays reveal that BbCOMMD6 interacts with the creatine kinase (CK), an essential enzyme involved in energy metabolism, forming a heterodimer BbCOMMD6-CK. The enzymatic activity assays show that CK activities are inhibited by BbCOMMD6 in a dose-dependent manner. All these data suggest that BbCOMMD6 is involved in energy transduction, via binding to CK and inhibiting activities of CK, and offer first clues to its role as a regulator of CK activities. |
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