| First Author | Wei Z | Year | 2015 |
| Journal | Biochem Biophys Res Commun | Volume | 456 |
| Issue | 3 | Pages | 750-6 |
| PubMed ID | 25514038 | Mgi Jnum | J:220363 |
| Mgi Id | MGI:5634260 | Doi | 10.1016/j.bbrc.2014.12.035 |
| Citation | Wei Z, et al. (2015) The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and sufficient for its caveolae-association. Biochem Biophys Res Commun 456(3):750-6 |
| abstractText | PTRF/cavin-1 is a protein of two lives. Its reported functions in ribosomal RNA synthesis and in caveolae formation happen in two different cellular locations: nucleus vs. plasma membrane. Here, we identified that the N-terminal leucine-zipper motif in PTRF/cavin-1 was essential for the protein to be associated with caveolae in plasma membrane. It could counteract the effect of nuclear localization sequence in the molecule (AA 235-251). Deletion of this leucine-zipper motif from PTRF/cavin-1 caused the mutant to be exclusively localized in nuclei. The fusion of this leucine-zipper motif with histone 2A, which is a nuclear protein, could induce the fusion protein to be exported from nucleus. Cell migration was greatly inhibited in PTRF/cavin-1(-/-) mouse embryonic fibroblasts (MEFs). The inhibited cell motility could only be rescued by exogenous cavin-1 but not the leucine-zipper motif deleted cavin-1 mutant. Plasma membrane dynamics is an important factor in cell motility control. Our results suggested that the membrane dynamics in cell migration is affected by caveolae associated PTRF/cavin-1. |
