Open AccessCalcineurin Colocalizes with P-Bodies and Stress Granules during Thermal Stress in Cryptococcus neoformans
Author(s) -
Lukasz Kozubowski,
Eanas F. Aboobakar,
María E. Cárdenas,
Joseph Heitman
Publication year - 2011
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.05087-11
Subject(s) - calcineurin , stress granule , biology , cryptococcus neoformans , unfolded protein response , endoplasmic reticulum , microbiology and biotechnology , transcription factor , poly(a) binding protein , phosphatase , transcription (linguistics) , serine , protein subunit , messenger rna , biochemistry , rna binding protein , phosphorylation , translation (biology) , gene , medicine , linguistics , philosophy , surgery , transplantation
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 pathogenCryptococcus 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.