Lap4, a vacuolar aminopeptidase I, is involved in cadmium-glutathione metabolism

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
Paula D B AdamisElis C A Eleutherio

Abstract

In Saccharomyces cerevisiae, accumulation of cadmium-glutathione complex in cytoplasm inhibits cadmium absorption, glutathione transferase 2 is required for the formation of the complex and the vacuolar gamma-glutamyl transferase participates of the first step of glutathione degradation. Here, we proposed that Lap4, a vacuolar amino peptidase, is involved in glutathione catabolism under cadmium stress. Saccharomyces cerevisiae cells deficient in Lap4 absorbed almost 3-fold as much cadmium as the wild-type strain (wt), probably due to the lower rate of cadmium-glutathione complex synthesis in the cytoplasm. In wt, but not in lap4 strain, the oxidized/reduced GSH ratio and the Gtt activity increased in response to cadmium, confirming that the mutant is deficient in the synthesis of the complex probably because the degradation of vacuolar glutathione is impaired. Thus, under cadmium stress, Lap4 and gamma-glutamyl transferase seem to work together to assure an efficient glutathione turnover stored in the vacuole.

References

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Citations

Nov 10, 2009·Phytochemistry·Jana WünschmannKlaus J Lendzian
May 21, 2014·Cellular Logistics·Karen A HechtJeffrey L Brodsky
Aug 8, 2018·FEMS Microbiology Letters·Zhiwei HuangPing Shi
Nov 14, 2018·Autophagy·Katherine R Parzych, Daniel J Klionsky
Dec 5, 2019·Proceedings of the National Academy of Sciences of the United States of America·Aline de Araújo BrasilElis Cristina Araujo Eleutherio

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