Calcineurin colocalizes with P-bodies and stress granules during thermal stress in Cryptococcus neoformans.


Journal Article

Calcineurin is a calcium-calmodulin-activated serine/threonine-specific phosphatase that operates during cellular responses to stress and plays a prominent role in transcriptional control, whereas regulatory events beyond transcription are less well characterized. This study reveals a novel transcription-independent role of calcineurin during the temperature stress response in the human fungal pathogen Cryptococcus neoformans. The diffusely cytoplasmic calcineurin catalytic subunit Cna1 relocates to endoplasmic reticulum (ER)-associated puncta and the mother-bud neck when cells are subjected to 37°C. More than 50% of Cna1 puncta contain the P-body constituent decapping enzyme Dcp1 and the stress granule constituent poly(A)-binding protein Pub1. These results support a model in which calcineurin orchestrates thermal stress responses by associating with sites of mRNA processing.

Full Text

Duke Authors

Cited Authors

  • Kozubowski, L; Aboobakar, EF; Cardenas, ME; Heitman, J

Published Date

  • November 2011

Published In

Volume / Issue

  • 10 / 11

Start / End Page

  • 1396 - 1402

PubMed ID

  • 21724937

Pubmed Central ID

  • 21724937

Electronic International Standard Serial Number (EISSN)

  • 1535-9786

Digital Object Identifier (DOI)

  • 10.1128/EC.05087-11


  • eng

Conference Location

  • United States