Genetic and physical interaction of Ssp1 CaMKK and Rad24 14-3-3 during low pH and osmotic stress in fission yeast.
Open Biol
; 4: 130127, 2014 Jan 22.
Article
en En
| MEDLINE
| ID: mdl-24451546
ABSTRACT
The Ssp1 calmodulin kinase kinase (CaMKK) is necessary for stress-induced re-organization of the actin cytoskeleton and initiation of growth at the new cell end following division in Schizosaccharomyces pombe. In addition, it regulates AMP-activated kinase and functions in low glucose tolerance. ssp1(-) cells undergo mitotic delay at elevated temperatures and G2 arrest in the presence of additional stressors. Following hyperosmotic stress, Ssp1-GFP forms transient foci which accumulate at the cell membrane and form a band around the cell circumference, but not co-localizing with actin patches. Hyperosmolarity-induced localization to the cell membrane occurs concomitantly with a reduction of its interaction with the 14-3-3 protein Rad24, but not Rad25 which remains bound to Ssp1. The loss of rad24 in ssp1(-) cells reduces the severity of hyperosmotic stress response and relieves mitotic delay. Conversely, overexpression of rad24 exacerbates stress response and concomitant cell elongation. rad24(-) does not impair stress-induced localization of Ssp1 to the cell membrane, however this response is almost completely absent in cells overexpressing rad24.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Schizosaccharomyces
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Proteínas HSP70 de Choque Térmico
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Proteínas de Ciclo Celular
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Proteínas de Schizosaccharomyces pombe
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Péptidos y Proteínas de Señalización Intracelular
Idioma:
En
Revista:
Open Biol
Año:
2014
Tipo del documento:
Article