Sorting Signals in the Cytosolic Tail of Plant p24 Proteins Involved in the Interaction with the COPII Coat
Author(s) -
Inmaculada Contreras,
Yaodong Yang,
David G. Robinson,
Fernando Aniento
Publication year - 2004
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/pch200
Subject(s) - copii , coat , sorting , protein targeting , cytosol , microbiology and biotechnology , coat protein , chemistry , biology , biophysics , biochemistry , membrane protein , endoplasmic reticulum , membrane , computer science , golgi apparatus , gene , secretory pathway , rna , enzyme , paleontology , programming language
The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cytosol.
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