Identification of striated muscle activator of Rho signaling (STARS) as a novel calmodulin target by a newly developed genome-wide screen
| Autor: | Kyohei Sakane, Tomoko Ogusu, Sumio Takahashi, Yusui Furuya, Naoki Kanayama, Miwako Denda, Ryo Morishita, Hiroshi Tokumitsu, Masaki Magari |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
animal structures Myosin light-chain kinase Calmodulin Physiology Amino Acid Motifs LIM-Homeodomain Proteins Plasma protein binding Biology Transfection Protein–protein interaction 03 medical and health sciences 0302 clinical medicine Chlorocebus aethiops Protein Interaction Mapping Animals Humans Genetic Testing Molecular Biology CAMK Transcription factor COS cells Genome Activator (genetics) Microfilament Proteins Cell Biology Molecular biology Cell biology Rats 030104 developmental biology COS Cells biology.protein Calcium 030217 neurology & neurosurgery Protein Binding Transcription Factors |
| Zdroj: | Cell calcium. 60(1) |
| ISSN: | 1532-1991 |
| Popis: | To search for novel target(s) of the Ca(2+)-signaling transducer, calmodulin (CaM), we performed a newly developed genome-wide CaM interaction screening of 19,676 GST-fused proteins expressed in human. We identified striated muscle activator of Rho signaling (STARS) as a novel CaM target and characterized its CaM binding ability and found that the Ca(2+)/CaM complex interacted stoichiometrically with the N-terminal region (Ala13-Gln35) of STARS in vitro as well as in living cells. Mutagenesis studies identified Ile20 and Trp33 as the essential hydrophobic residues in CaM anchoring. Furthermore, the CaM binding deficient mutant (Ile20Ala, Trp33Ala) of STARS further enhanced its stimulatory effect on SRF-dependent transcriptional activation. These results suggest a connection between Ca(2+)-signaling via excitation-contraction coupling and the regulation of STARS-mediated gene expression in muscles. |
| Databáze: | OpenAIRE |
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