| First Author | Loomis PA | Year | 2006 |
| Journal | J Cell Sci | Volume | 119 |
| Issue | Pt 8 | Pages | 1655-65 |
| PubMed ID | 16569662 | Mgi Jnum | J:107807 |
| Mgi Id | MGI:3622040 | Doi | 10.1242/jcs.02869 |
| Citation | Loomis PA, et al. (2006) Targeted wild-type and jerker espins reveal a novel, WH2-domain-dependent way to make actin bundles in cells. J Cell Sci 119(Pt 8):1655-65 |
| abstractText | The espin actin-bundling proteins, which are the target of deafness mutations, are present in the parallel actin bundles of stereocilia and microvilli and appear to increase their steady-state length. Here, we report a new activity of the espins, one that depends on their enigmatic WH2 domain: the ability to assemble a large actin bundle when targeted to a specific subcellular location. This activity was observed for wild-type espins targeted to the centrosome in transfected neuronal cells and for jerker espins targeted to the nucleolus in a wide variety of transfected cells as a result of the frameshifted peptide introduced into the espin C-terminus by the jerker deafness mutation. This activity, which appears specific to espins, requires two espin F-actin-binding sites and the actin-monomer-binding activity of the espin WH2 domain, but can be mimicked by adding a WH2 domain to an unrelated actin-bundling protein, villin. Espins do not activate the Arp2/3 complex in vitro, and bundle assembly is not indicative of in-vitro nucleation activity. Our results suggest a novel way to build actin bundles at specific sites in cells. |
