RRC ID 50372
Author Hoya M, Yanguas F, Moro S, Prescianotto-Baschong C, Doncel C, de León N, Curto MÁ, Spang A, Valdivieso MH.
Title Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast.
Journal Genetics
Abstract Despite its biological and medical relevance, traffic from the Golgi to the plasma membrane (PM) is one of the least understood steps of secretion. Exomer is a protein complex that mediates the trafficking of certain cargoes from the trans-Golgi network/early endosomes to the PM in budding yeast. Here, we show that in Schizosaccharomyces pombe the Cfr1 and Bch1 proteins constitute the simplest form of an exomer. Cfr1 co-immunoprecipitates with Assembly Polypeptide adaptor 1 (AP-1), AP-2, and Golgi-localized, gamma-adaptin ear domain homology, ARF-binding (GGA) subunits, and cfr1+ interacts genetically with AP-1 and GGA genes. Exomer-defective cells exhibit multiple mild defects, including alterations in the morphology of Golgi stacks and the distribution of the synaptobrevin-like Syb1 protein, carboxypeptidase missorting, and stress sensitivity. S. pombe apm1Δ cells exhibit a defect in trafficking through the early endosomes that is severely aggravated in the absence of exomer. apm1Δ cfr1Δ cells exhibit a dramatic disorganization of intracellular compartments, including massive accumulation of electron-dense tubulovesicular structures. While the trans-Golgi network/early endosomes are severely disorganized in the apm1Δ cfr1Δ strain, gga21Δ gga22Δ cfr1Δ cells exhibit a significant disturbance of the prevacuolar/vacuolar compartments. Our findings show that exomer collaborates with clathrin adaptors in trafficking through diverse cellular compartments, and that this collaboration is important to maintain their integrity. These results indicate that the effect of eliminating exomer is more pervasive than that described to date, and suggest that exomer complexes might participate in diverse steps of vesicle transport in other organisms.
Volume 205(2)
Pages 673-690
Published 2017-2
DOI 10.1534/genetics.116.193458
PII genetics.116.193458
PMID 27974503
PMC PMC5289844
MeSH Adaptor Protein Complex 1 / genetics Adaptor Protein Complex 1 / metabolism* Adaptor Protein Complex 2 / genetics Adaptor Protein Complex 2 / metabolism* Adaptor Proteins, Vesicular Transport / genetics* Adaptor Proteins, Vesicular Transport / metabolism Endosomes / metabolism* Protein Binding Protein Transport R-SNARE Proteins / genetics R-SNARE Proteins / metabolism Schizosaccharomyces / genetics Schizosaccharomyces / metabolism* Schizosaccharomyces pombe Proteins / genetics* Schizosaccharomyces pombe Proteins / metabolism trans-Golgi Network / metabolism*
IF 3.564
Times Cited 0
Yeast FY23692 FY12296(HVP2032) FY6924(HVP4183) FY23767(HVP4022)