title: Proteomics on brefeldin A-treated Arabidopsis roots reveals profilin 2 as a new protein involved in the cross-talk between vesicular trafficking and the actin cytoskeleton.
abstract: The growing importance of vesicular trafficking and cytoskeleton dynamic reorganization during plant development requires the exploitation of novel experimental approaches. Several genetic and cell biological studies have used diverse pharmaceutical drugs that inhibit vesicular trafficking and secretion to study these phenomena. Here, proteomic and cell biology approaches were applied to study effects of brefeldin A (BFA), an inhibitor of vesicle recycling and secretion, in Arabidopsis roots. The main aim of this study was to obtain an overview of proteins affected by BFA, but especially to identify new proteins involved in the vesicular trafficking and its cross-talk to the actin cytoskeleton. The results showed that BFA altered vesicular trafficking and caused the formation of BFA-compartments which was accompanied by differential expression of several proteins in root cells. Some of the BFA-up-regulated proteins belong to the class of the vesicular trafficking proteins, such as V-ATPase and reversibly glycosylated polypeptide, while others, such as profilin 2 and elongation factor 1 alpha, are rather involved in the remodeling of the actin cytoskeleton. Upregulation of profilin 2 by BFA was verified by immunoblot and live imaging at subcellular level. The latter approach also revealed that profilin 2 accumulated in BFA-compartments which was accompanied by remodeling of the actin cytoskeleton in BFA-treated root cells. Thus, profilin 2 seems to be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton, in a BFA-dependent manner.
authors.affiliation: Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Department of Cell Biology, Palacký University, Olomouc, Czech Republic. tomas.takac@upol.cz
authors.forename: Tomás
authors.initials: T
authors.lastname: Takác
authors.forename: Tibor
authors.initials: T
authors.lastname: Pechan
authors.forename: Hendrik
authors.initials: H
authors.lastname: Richter
authors.forename: Jens
authors.initials: J
authors.lastname: Müller
authors.forename: Carola
authors.initials: C
authors.lastname: Eck
authors.forename: Nils
authors.initials: N
authors.lastname: Böhm
authors.forename: Bohus
authors.initials: B
authors.lastname: Obert
authors.forename: Haiyun
authors.initials: H
authors.lastname: Ren
authors.forename: Karsten
authors.initials: K
authors.lastname: Niehaus
authors.forename: Jozef
authors.initials: J
authors.lastname: Samaj
mesh_terms: D000199:Actins / Q000378:metabolism; D017360:Arabidopsis / Q000187:drug effects* / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D020126:Brefeldin A / Q000494:pharmacology*; D003599:Cytoskeleton / Q000187:drug effects; D015180:Electrophoresis, Gel, Two-Dimensional; D010940:Plant Proteins / Q000032:analysis / Q000378:metabolism; D018517:Plant Roots / Q000166:cytology / Q000378:metabolism; D051304:Profilins / Q000378:metabolism*; D021381:Protein Transport / Q000187:drug effects; D020543:Proteome / Q000032:analysis / Q000378:metabolism*; D040901:Proteomics; D015398:Signal Transduction / Q000187:drug effects; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D000199:Actins; D029681:Arabidopsis Proteins; C495747:PRF2 protein, Arabidopsis; D010940:Plant Proteins; D051304:Profilins; D020543:Proteome; D020126:Brefeldin A