Hardin Jeff
Department of Zoology, University of Wisconsin-Madison, Madison, WI, USA.
F1000Res. 2015 Dec 18;4. doi: 10.12688/f1000research.6866.1. eCollection 2015.
The classic cadherin-catenin complex (CCC) mediates cell-cell adhesion in metazoans. Although substantial insights have been gained by studying the CCC in vertebrate tissue culture, analyzing requirements for and regulation of the CCC in vertebrates remains challenging. Caenorhabditis elegans is a powerful system for connecting the molecular details of CCC function with functional requirements in a living organism. Recent data, using an "angstroms to embryos" approach, have elucidated functions for key residues, conserved across all metazoans, that mediate cadherin/β-catenin binding. Other recent work reveals a novel, potentially ancestral, role for the C. elegans p120ctn homologue in regulating polarization of blastomeres in the early embryo via Cdc42 and the partitioning-defective (PAR)/atypical protein kinase C (aPKC) complex. Finally, recent work suggests that the CCC is trafficked to the cell surface via the clathrin adaptor protein complex 1 (AP-1) in surprising ways. These studies continue to underscore the value of C. elegans as a model system for identifying conserved molecular mechanisms involving the CCC.
经典钙黏蛋白-连环蛋白复合体（CCC）介导后生动物中的细胞间黏附。尽管通过在脊椎动物组织培养中研究CCC已获得了大量见解，但分析脊椎动物中CCC的需求和调控仍然具有挑战性。秀丽隐杆线虫是一个强大的系统，可将CCC功能的分子细节与活生物体中的功能需求联系起来。最近的数据采用了一种“从埃到胚胎”的方法，阐明了所有后生动物中保守的关键残基的功能，这些残基介导钙黏蛋白/β-连环蛋白结合。其他近期研究揭示了秀丽隐杆线虫p120ctn同源物通过Cdc42和PAR/非典型蛋白激酶C（aPKC）复合体在调节早期胚胎中卵裂球极化方面的一种新的、可能是祖先的作用。最后，近期研究表明，CCC以令人惊讶的方式通过网格蛋白衔接蛋白复合体1（AP-1）转运到细胞表面。这些研究继续强调秀丽隐杆线虫作为鉴定涉及CCC的保守分子机制的模型系统的价值。
