Interaction between ESCRT-III proteins and the yeast SERINC homolog Tms1.

The endosomal sorting complex required for transport (ESCRT)-III is involved in membrane remodeling and abscission during intraluminal vesicle (ILV) formation at endosomes. Our data now suggest that ESCRT-III function could be connected to lipid remodeling of the endosomal membrane. This notion is based on our finding that ESCRT-III proteins bind to the yeast serine incorporator (SERINC) homolog Tms1.

Investigation of stress tolerance of Pichia kudriavzevii for high gravity bioethanol production from steam-exploded wheat straw hydrolysate.

This study investigated a newly isolated thermotolerant strain of Pichia kudriavzevii with respect to its stress tolerance and fermentation performance. Response surface methodology was applied to evaluate the combined effects of furfural, osmotic and thermal stress on ethanol yield. The proposed model shows that P.

Vps68 cooperates with ESCRT-III in intraluminal vesicle formation.

The endosomal sorting complex required for transport (ESCRT)-III mediates budding and abscission of intraluminal vesicles (ILVs) into multivesicular endosomes. To further define the role of the yeast ESCRT-III-associated protein Mos10 (also known as Vps60) in ILV formation, we screened for new interaction partners by using stable isotope labeling of amino acids in cell culture (SILAC) and mass spectrometry. Here, we focused on the newly identified interaction partner Vps68.

Comprehensive analysis of yeast ESCRT-III composition in single ESCRT-III deletion mutants.

The endosomal sorting complex required for transport (ESCRT)-III is associated with a multitude of cellular processes involving membrane remodeling and abscission. The exact composition of ESCRT-III and the contribution of individual ESCRT-III family members to these diverse functions is unclear. Most of the currently available information about ESCRT-III was obtained with tagged, largely non-functional proteins, which may not correctly reflect the situation.

Interactions in the ESCRT-III network of the yeast Saccharomyces cerevisiae.

Here, we examine the genetic interactions between ESCRT-III mutations in the yeast Saccharomyces cerevisiae. From the obtained interaction network, we make predictions about alternative ESCRT-III complexes. By the successful generation of an octuple deletion strain using the CRISPR/Cas9 technique, we demonstrate for the first time that ESCRT-III activity as a whole is not essential for the life of a yeast cell.