Open AccessECERIFERUM11/C-TERMINAL DOMAIN PHOSPHATASE-LIKE2 Affects Secretory Trafficking
Author(s) -
Lin Shi,
Gillian H. Dean,
Huanquan Zheng,
Miranda J. Meents,
Tegan M. Haslam,
George W. Haughn,
Ljerka Kunst
Publication year - 2019
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.19.00722
Subject(s) - secretion , microbiology and biotechnology , arabidopsis , arabidopsis thaliana , secretory pathway , secretory protein , dephosphorylation , biology , extracellular , phosphatase , extracellular matrix , chemistry , biochemistry , phosphorylation , mutant , gene , golgi apparatus , endoplasmic reticulum
Secretory trafficking is highly conserved in all eukaryotic cells and is required for secretion of proteins as well as extracellular matrix components. In plants, the export of cuticular waxes and various cell wall components relies on secretory trafficking, but the molecular mechanisms underlying their secretion are not well understood. In this study, we characterize the Arabidopsis ( Arabidopsis thaliana ) dwarf eceriferum11 ( cer11 ) mutant and we show that it exhibits reduced stem cuticular wax deposition, aberrant seed coat mucilage extrusion, and delayed secondary cell wall columella formation, as well as a block in secretory GFP trafficking. Cloning of the CER11 gene revealed that it encodes a C-TERMINAL DOMAIN PHOSPHATASE-LIKE2 (CPL2) protein. Thus, secretory trafficking in plant cells in general, and secretion of extracellular matrix constituents in developing epidermal cells in particular, involves a dephosphorylation step catalyzed by CER11/CPL2.
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