| First Author | Lederer M | Year | 2005 |
| Journal | J Cell Sci | Volume | 118 |
| Issue | Pt 2 | Pages | 331-41 |
| PubMed ID | 15615774 | Mgi Jnum | J:95526 |
| Mgi Id | MGI:3526474 | Doi | 10.1242/jcs.01618 |
| Citation | Lederer M, et al. (2005) Profilin regulates the activity of p42POP, a novel Myb-related transcription factor. J Cell Sci 118(Pt 2):331-41 |
| abstractText | Profilins, regulators of cytoplasmic actin dynamics, also bind to several nuclear proteins but the significance of these interactions is mostly unclear. Here, we describe a novel Myb-related transcription factor, p42(POP), as a new ligand for profilin and show that profilin regulates its activity. p42(POP) comprises a unique combination of domains and is widely expressed in mouse tissues. In contrast to many other Myb proteins, it contains only one functional tryptophan-cluster motif. This is followed by an acidic domain, a leucine zipper that mediates dimerization and functional nuclear import and export signals that can direct p42(POP) to either the nuclear or the cytoplasmic compartment. Binding to profilins is mediated by a proline-rich cluster. p42(POP)-profilin complexes can be precipitated from cell lysates. In transfected cells displaying p42(POP) in the nucleus, nuclear profilin is markedly increased. When p42(POP) is anchored at mitochondrial membranes, profilin is targeted to this location. Hence, in a cellular environment, p42(POP) and profilin are found in the same protein complex. In luciferase assays, p42(POP) acts as repressor and this activity is substantially reduced by profilins, indicating that profilin can regulate p42(POP) activity and is therefore involved in gene regulation. |
