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Updated: May 21, 2026

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
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Interaction between Rsp5-dependent ubiquitination and trehalose production during Cryptococcus neoformans temperature

Alejandro L Antonia1,2, Lukas M du Plooy1,2, Siobhan R Duffy1,2

  • 1Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA.

Msphere
|May 20, 2026
PubMed
Summary

The opportunistic fungus Cryptococcus neoformans uses Rsp5-dependent ubiquitination to regulate trehalose biosynthesis, enhancing survival against temperature and salt stress during human infections.

Keywords:
Cryptococcus neoformansfungal pathogenesisosmotic stressstress responsetemperature stresstrehaloseubiquitination

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Last Updated: May 21, 2026

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Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
09:27

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Published on: February 17, 2017

Area of Science:

  • Microbiology
  • Molecular Biology
  • Mycology

Background:

  • * Cryptococcus neoformans* is an opportunistic fungal pathogen causing significant mortality.
  • * C. neoformans* must adapt to host environmental stressors like elevated temperature and osmotic stress.
  • * The HECT E3-ubiquitin ligase Rsp5 is crucial for stress tolerance in *C. neoformans*.

Purpose of the Study:

  • * To elucidate the substrates and mechanisms regulated by Rsp5 in *C. neoformans* stress response.
  • * To investigate the role of Rsp5 in regulating trehalose biosynthesis pathway.
  • * To understand how Rsp5-mediated ubiquitination contributes to fungal survival in host environments.

Main Methods:

  • * Quantitative proteomic analysis of *C. neoformans* under high salinity.
  • * Measurement of trehalose production following high-temperature stress.
  • * Analysis of ubiquitination patterns of trehalose biosynthesis enzymes Tps1 and Tps2.

Main Results:

  • * Rsp5 regulates the trehalose biosynthesis pathway, impacting stress tolerance.
  • * Tps1 and Tps2 enzymes are differentially ubiquitinated by Rsp5 upon stress exposure.
  • * *C. neoformans* strains lacking Rsp5 exhibit impaired trehalose production and reduced stress tolerance.
  • * Rsp5-dependent ubiquitination of Tps1/Tps2 does not alter their protein abundance.

Conclusions:

  • * Rsp5-dependent ubiquitination of trehalose biosynthesis enzymes is a key mechanism for *C. neoformans* survival under host-relevant stress conditions.
  • * This regulation of trehalose production contributes to the pathogen's ability to proliferate in mammalian hosts.
  • * Understanding Rsp5's role in stress adaptation may reveal new therapeutic targets against *C. neoformans* infections.