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Mutations affecting phosphorylation, ubiquitination and turnover of the ABC‐transporter Ste6
Author(s) -
Kölling Ralf
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03621-9
Subject(s) - phosphorylation , ubiquitin , transporter , atp binding cassette transporter , chemistry , microbiology and biotechnology , biochemistry , biology , gene
In this report, the role of phosphorylation in the regulation of ubiquitination and turnover of the ABC‐transporter Ste6 was investigated. We demonstrate that Ste6 is phosphorylated in vivo and that this phosphorylation is dependent on the presence of an acidic stretch (‘A‐box’) in the linker region previously shown to be important for ubiquitination and fast turnover of Ste6. By mutagenesis, two serine/threonine residues were identified in the A‐box region that are crucial for ubiquitination and trafficking to the yeast vacuole. In the mutants there was no simple correlation between phosphorylation and ubiquitination levels, suggesting that the two events may not be coupled.