Loss of a GPI-anchored membrane protein Aah3p causes a defect in vacuolar protein sorting in Schizosaccharomyces pombe.

نویسندگان

  • Tomoko Iwaki
  • Tomotake Morita
  • Naotaka Tanaka
  • Yuko Giga-Hama
  • Kaoru Takegawa
چکیده

Schizosaccharomyces pombe has four alpha-amylase homologs (Aah1p-Aah4p) with a glycosylphosphatidylinositol (GPI) modification site at the C-terminal end. Disruption mutants of aah genes were tested for mislocalization of vacuolar carboxypeptidase Y (CPY), and aah3Delta was found to secrete CPY. The conversion rate from pro- to mature CPY was greatly impaired in aah3Delta, and fluorescence microscopy inidicated that a sorting receptor for CPY, Vps10p, mislocalized to the vacuolar membrane. These results indicate that aah3Delta had a defect in the retrograde transport of Vps10p, and that Aah3p is the first S. pombe specific protein required for vacuolar protein sorting.

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عنوان ژورنال:
  • Bioscience, biotechnology, and biochemistry

دوره 71 2  شماره 

صفحات  -

تاریخ انتشار 2007