| First Author | Doucet J | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 290 |
| Issue | 2 | Pages | 783-9 |
| PubMed ID | 11785969 | Mgi Jnum | J:73927 |
| Mgi Id | MGI:2157200 | Doi | 10.1006/bbrc.2001.6236 |
| Citation | Doucet J, et al. (2002) Molecular cloning and functional characterization of mouse coactosin-like protein. Biochem Biophys Res Commun 290(2):783-9 |
| abstractText | Coactosin was first isolated from Dictyostelium discoideum and, as reported, human coactosin-like protein (CLP) was identified in a yeast two-hybrid screen using 5-lipoxygenase (5LO) as a bait. A mouse CLP (mCLP) cDNA clone was identified among EMBL/GenBank EST sequences. The derived amino acid sequence (142 residues) was 95.1% identical with human CLP. Here, we also show that mCLP interacts with actin and 5LO in the two-hybrid system. High-speed cosedimentation assays and GST-binding assays confirmed these protein interactions. In chemical cross-linking experiments, one molecule of mCLP was covalently linked to either one subunit of actin or one molecule of 5LO. The mCLP-F-actin and mCLP-5LO associations were pH-insensitive and Ca(2+)-independent. However, association with actin was best observed at low salt concentrations, while association with 5LO was favored by salt, indicating different binding characteristics. |
