| First Author | Muccioli M | Year | 2016 |
| Journal | Dev Biol | Volume | 412 |
| Issue | 1 | Pages | 32-43 |
| PubMed ID | 26902112 | Mgi Jnum | J:231604 |
| Mgi Id | MGI:5771937 | Doi | 10.1016/j.ydbio.2016.02.016 |
| Citation | Muccioli M, et al. (2016) Lens placode planar cell polarity is dependent on Cdc42-mediated junctional contraction inhibition. Dev Biol 412(1):32-43 |
| abstractText | Development of the ocular lens commences with the formation of the lens placode, an epithelial structure that thickens and subsequently bends inward in a process called invagination. Invagination is observed during the development of many embryonic structures, but the spectrum of morphogenetic events driving this process are, in most cases, not fully understood. A characteristic commonly found in embryonic tissues undergoing epithelial reorganization is planar polarity, a property where cells are geometrically and/or molecularly orientated in a specific direction along the plane of an epithelium. Planar polarity is known to drive the morphogenesis of several epithelial structures, however its role during invagination events is less clear. We have found that at the onset of invagination, cells of the lens placode become geometrically planar polarized such that they are orientated toward a central point in the lens placode. Further investigation revealed that this is due to contraction of radially orientated junctions and the elongation of those circumferentially orientated. Radial junctions have an elevated localization of actomyosin and their contraction is dependent on the F-actin and Rho-kinase binding protein, Shroom3. Elongation of circumferential junctions is dependent upon Cdc42, a Rho-GTPase known to regulate polarity via the Par-complex. We determined that Cdc42 and members of the Par-complex inhibit Shroom3-induced contractility and promote anisotropic placode cell geometry through inhibition of junctional contraction. We postulate that invagination of the lens placode requires careful orchestration of these opposing processes which are mediated by the planar polarization of junctional proteins. |
