Tiki1 Is Required for Head Formation via Wnt Cleavage-Oxidation and Inactivation

Zhang, Xinjun; Abreu, José G.; Yokota, Chika; MacDonald, Bryan T.; Singh, Sasha A; Coburn, Karla Loureiro Almeida; Cheong, Seong Moon; Zhang, Mingzi M.; Ye, Qi Zhuang; Hang, Howard C.; Steen, Hanno; He, Xi

doi:10.1016/j.cell.2012.04.039

Cited by 129 publications

(212 citation statements)

References 43 publications

(56 reference statements)

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“…Wnt family members are essential for embryogenesis, pathogenesis, and regeneration, and like Hhs, palmitoylated Wnt proteins initially locate to the cell surface and require solubilization to reach their targets. In this process, Wnts can undergo proteolysis-induced processing of eight N-terminal amino acids, resulting in Wnt oxidation oligomerization and functional inactivation (69). Therefore, Wnts and Shh represent two examples for the emerging theme of functional morphogen control by proteolytic removal of regulatory N-terminal peptides.…”

Section: Discussionmentioning

confidence: 99%

An Emerging Role of Sonic Hedgehog Shedding as a Modulator of Heparan Sulfate Interactions

Ohlig

Pickhinke

Sirko

et al. 2012

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

An Emerging Role of Sonic Hedgehog Shedding as a Modulator of Heparan Sulfate Interactions

Ohlig

Pickhinke

Sirko

et al. 2012

Journal of Biological Chemistry

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“…Wnt proteins are ϳ350 amino acids in size and cysteine-rich and undergo several post-translational modifications during biogenesis, including the addition of a palmitoleic acid moiety, multiple N-glycosylations, and the coordination of a series of disulfide bonds (4,5). The human genome encodes 19 WNT proteins, which can be divided into 12 paralogous groups (6) and have been shown to signal through a multitude of seventransmembrane Frizzled receptors (FZD1 to -10) and singletransmembrane Wnt receptors or coreceptors, including LRP5/6, ROR1/2, RYK, and others (7,8). It is generally thought that the receptor complex dictates the signaling pathway choice initiated by the Wnt ligand, as best illustrated in the case of FZD and LRP5/6 for ␤-catenin signaling (1).…”

mentioning

confidence: 99%

Disulfide Bond Requirements for Active Wnt Ligands

MacDonald

Hien

Zhang

et al. 2014

Journal of Biological Chemistry

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Background: Wnt proteins are rich in cysteines, but their functional significance has not been systematically examined. Results: Mutagenesis of cysteines in Wnt3a uncovers their requirements for Wnt secretion and/or receptor binding. Conclusion: Behaviors of the Wnt3a cysteine mutants are consistent with the Wnt structure model. Significance: This study provides insights into pathogenesis associated with WNT mutations and new tool sets for WNT research.

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“…Zhang et.al. (45) identified Tiki as a protease family playing a critical role in cell growth and development via specific cleavage of the Wnt protein (45). PrgY is homologous to the human Tiki metalloprotease, both having a pair of GX 2 H motifs and a conserved glutamate residue, and it is predicted to have structural similarity to the so-called EraA/ChaN-like family of proteins (46).…”

Section: How and Why Did The Pcf10 System Become So Complex?mentioning

confidence: 99%

Enterococcal Sex Pheromones: Evolutionary Pathways to Complex, Two-Signal Systems

Dunny

Berntsson

2016

J Bacteriol

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bGram-positive bacteria carry out intercellular communication using secreted peptides. Important examples of this type of communication are the enterococcal sex pheromone systems, in which the transfer of conjugative plasmids is controlled by intercellular signaling among populations of donors and recipients. This review focuses on the pheromone response system of the conjugative plasmid pCF10. The peptide pheromones regulating pCF10 transfer act by modulating the ability of the PrgX transcription factor to repress the transcription of an operon encoding conjugation functions. Many Gram-positive bacteria regulate important processes, including the production of virulence factors, biofilm formation, sporulation, and genetic exchange using peptide-mediated signaling systems. The key master regulators of these systems comprise the RRNPP (RggRap/NprR/ PlcR/PrgX) family of intracellular peptide receptors; these regulators show conserved structures. While many RRNPP systems include a core module of two linked genes encoding the regulatory protein and its cognate signaling peptide, the enterococcal sex pheromone plasmids have evolved to a complex system that also recognizes a second host-encoded signaling peptide. Additional regulatory genes not found in most RRNPP systems also modulate signal production and signal import in the enterococcal pheromone plasmids. This review summarizes several structural studies that cumulatively demonstrate that the ability of three pCF10 regulatory proteins to recognize the same 7-amino-acid pheromone peptide arose by convergent evolution of unrelated proteins from different families. We also focus on the selective pressures and structure/function constraints that have driven the evolution of pCF10 from a simple, single-peptide system resembling current RRNPPs in other bacteria to the current complex inducible plasmid transfer system. BACKGROUND AND SIGNIFICANCE

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Tiki1 Is Required for Head Formation via Wnt Cleavage-Oxidation and Inactivation

Cited by 129 publications

References 43 publications

An Emerging Role of Sonic Hedgehog Shedding as a Modulator of Heparan Sulfate Interactions

An Emerging Role of Sonic Hedgehog Shedding as a Modulator of Heparan Sulfate Interactions

Disulfide Bond Requirements for Active Wnt Ligands

Enterococcal Sex Pheromones: Evolutionary Pathways to Complex, Two-Signal Systems

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