High impact information on VPS16

• Using an in vitro decapping assay, we have identified a factor, Vps16p, that regulates the activity of the yeast decapping enzyme, Dcp1p [1].
• The VPS16 gene product associates with a sedimentable protein complex and is essential for vacuolar protein sorting in yeast [2].
• To understand the role of the VPS16 gene in vacuolar protein sorting and organelle assembly, a vps16 ts mutant was used to clone the wild-type gene [2].
• The Saccharomyces cerevisiae vacuolar protein sorting mutant, vps16, exhibits pleiotropic defects in vacuolar protein targeting and vacuole morphology [2].
• DNA sequence analysis identified a single open reading frame within a vps16 complementing DNA fragment, capable of encoding a protein of 92,000 Da [2].

Biological context of VPS16

• Two independently isolated, temperature-sensitive strains that were also defective for karmellae biogenesis carried mutations in VPS16, a gene involved in vacuolar protein sorting [3].

Associations of VPS16 with chemical compounds

• This association is resistant to detergent and salt extractions, but Vps16p can be extracted with 6 M urea and alkali buffer [2].

Other interactions of VPS16

• The mutant vpt13 is deficient in vacuolar acidification but possesses a morphologically normal vacuole, whereas vpt16 is devoid of any vacuole-like structure [4].
• Mutations in vps16, vps18, and vps33 are known to result in decreased pigmentation in organisms such as Drosophila [5].

References