Association of Calcineurin with the COPI Protein Sec28 and the COPII Protein Sec13 Revealed by Quantitative Proteomics Calcineurin-Associated Proteome
2011

Calcineurin and Its Role in Protein Interactions in Cryptococcus neoformans

publication 10 minutes Evidence: moderate

Author Information

Author(s): Kozubowski Lukasz, Thompson J. Will, Cardenas Maria E., Moseley M. Arthur, Heitman Joseph

Primary Institution: Duke University Medical Center

Hypothesis

The study aims to identify proteins that associate with the calcineurin catalytic subunit Cna1 and their relevance to thermal stress response in Cryptococcus neoformans.

Conclusion

The study identifies several proteins that associate with calcineurin, suggesting its role in cellular stress responses and membrane trafficking.

Supporting Evidence

  • Calcineurin is essential for growth at high temperature and virulence of Cryptococcus neoformans.
  • Mass spectrometry identified 327 proteins associated with calcineurin.
  • Cna1 co-purified with proteins involved in membrane trafficking.
  • Calcineurin localization changes during high temperature stress.
  • Sec28 and Sec13 were confirmed as interacting proteins with Cna1.

Takeaway

This study found that a protein called calcineurin helps other proteins work together when the fungus Cryptococcus neoformans gets too hot.

Methodology

Mass spectrometry was used to identify proteins associated with calcineurin in Cryptococcus neoformans under different temperature conditions.

Limitations

The study may not have identified all calcineurin-associated proteins due to the nature of the mass spectrometry approach.

Statistical Information

P-Value

p<0.01

Statistical Significance

p<0.01

Digital Object Identifier (DOI)

10.1371/journal.pone.0025280

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