Schluter C~Conibear E, 2008

Pubmed ID 18216282
Title Global analysis of yeast endosomal transport identifies the vps55/68 sorting complex.
Authors Cayetana Schluter, Karen K Y Lam, Jochen Brumm, Bella W Wu, Matthew Saunders, Tom H Stevens, Jennifer Bryan, Elizabeth Conibear
Abstract Endosomal transport is critical for cellular processes ranging from receptor down-regulation and retroviral budding to the immune response. A full understanding of endosome sorting requires a comprehensive picture of the multiprotein complexes that orchestrate vesicle formation and fusion. Here, we use unsupervised, large-scale phenotypic analysis and a novel computational approach for the global identification of endosomal transport factors. This technique effectively identifies components of known and novel protein assemblies. We report the characterization of a previously undescribed endosome sorting complex that contains two well-conserved proteins with four predicted membrane-spanning domains. Vps55p and Vps68p form a complex that acts with or downstream of ESCRT function to regulate endosomal trafficking. Loss of Vps68p disrupts recycling to the TGN as well as onward trafficking to the vacuole without preventing the formation of lumenal vesicles within the MVB. Our results suggest the Vps55/68 complex mediates a novel, conserved step in the endosomal maturation process.
Citation Mol. Biol. Cell 2008; 19:1282-94

Datasets

Download the list of datasets
Papers Phenotype Conditions Collection Tested mutants Data Details
Schluter C~Conibear E, 2008 transport to/from cell surface (CPY) standard [standard] hap a 4,505 Quantitative
Schluter C~Conibear E, 2008 transport to/from cell surface (CPY) standard [standard] hap alpha 4,554 Quantitative
Schluter C~Conibear E, 2008 transport to/from cell surface (CPY) standard [standard] hom 4,632 Quantitative

Curation history

Data

Jan. 17, 2018 Data to load.
Jan. 19, 2018 Data loaded.

Tested strains

Jan. 17, 2018 Tested strains to load.
Jan. 19, 2018 Tested strains loaded.