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RISS 인기검색어
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- 저자 : Loveless, T. (검색결과 2 건)
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Shao, Xiangqiang,Kang, Hyunook,Loveless, Timothy,Lee, Gyu Rie,Seok, Chaok,Weis, William I.,Choi, Hee-Jung,Hardin, Jeff American Society for Biochemistry and Molecular Bi 2017 The Journal of biological chemistry Vol.292 No.40
<P>Stable tissue integrity during embryonic development relies on the function of the cadherin center dot catenin complex (CCC). The Caenorhabditis elegans CCC is a useful paradigm for analyzing in vivo requirements for specific interactions among the core components of the CCC, and it provides a unique opportunity to examine evolutionarily conserved mechanisms that govern the interaction between alpha- and beta-catenin. HMP-1, unlike its mammalian homolog alpha-catenin, is constitutively monomeric, and its binding affinity for HMP-2/beta-catenin is higher than that of alpha-catenin for beta-catenin. A crystal structure shows that the HMP-1 center dot HMP-2 complex forms a five-helical bundle structure distinct from the structure of the mammalian alpha-catenin beta-catenin complex. Deletion analysis based on the crystal structure shows that the first helix of HMP-1 is necessary for binding HMP-2 avidly in vitro and for efficient recruitment of HMP-1 to adherens junctions in embryos. HMP-2 Ser-47 and Tyr-69 flank its binding interface with HMP-1, and we show that phosphomimetic mutations at these two sites decrease binding affinity of HMP-1 to HMP-2 by 40-100-fold in vitro. In vivo experiments using HMP-2 S47E and Y69E mutants showed that they are unable to rescue hmp-2(zu364) mutants, suggesting that phosphorylation of HMP-2 on Ser-47 and Tyr-69 could be important for regulating CCC formation in C. elegans. Our data provide novel insights into how cadherin-dependent cell-cell adhesion is modulated in metazoans by conserved elements as well as features unique to specific organisms.</P>
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Choi, H.J.,Loveless, T.,Lynch, A.M.,Bang, I.,Hardin, J.,Weis, William I. Cell Press 2015 DEVELOPMENTAL CELL Vol.33 No.1
<P>In metazoan adherens junctions, beta-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein a-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for beta-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. Here, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the beta-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function ( Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for beta-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous beta-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Our structural data define critical sequence differences responsible for the unique ligand specificities of these two proteins.</P>
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