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• W2118846511 abstract "Cell-to-cell communication is essential for the coordinated development of multicellular organisms. Members of the CLAVATA3/EMBRYO-SURROUNDING REGION-RELATED (CLE) family, a group of small secretory peptides, are involved in these processes in plants. Although post-translational modifications are considered to be indispensable for their activity, the detailed mechanisms governing these modifications are not well understood. Here, we report that SUPPRESSOR OF LLP1 1 (SOL1), a putative Zn2+ carboxypeptidase previously isolated as a suppressor of the CLE19 over-expression phenotype, functions in C–terminal processing of the CLE19 proprotein to produce the functional CLE19 peptide. Newly isolated sol1 mutants are resistant to CLE19 over-expression, consistent with the previous report (Casamitjana-Martinez, E., Hofhuis, H.F., Xu, J., Liu, C.M., Heidstra, R. and Scheres, B. (2003) Curr. Biol. 13, 1435–1441). As expected, our experiment using synthetic CLE19 peptide revealed that the sol1 mutation does not compromise CLE signal transduction pathways per se. SOL1 possesses enzymatic activity to remove the C–terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C–terminal arginine residue is necessary for CLE19 activity in vivo. Additionally, the endosomal localization of SOL1 suggests that this processing occurs in endosomes in the secretory pathway. Thus, our data indicate the importance of C–terminal processing of CLE proproteins to ensure CLE activities." @default.
• W2118846511 created "2016-06-24" @default.
• W2118846511 creator A5005738882 @default.
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• W2118846511 date "2013-11-12" @default.
• W2118846511 modified "2023-10-02" @default.
• W2118846511 title "SUPPRESSOR OF LLP1 1-mediated C-terminal processing is critical for CLE19 peptide activity" @default.
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• W2118846511 doi "https://doi.org/10.1111/tpj.12349" @default.
• W2118846511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24118638" @default.
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