Abstract
Control of gene expression by stress-activated protein kinase (SAPK) cascades is crucial for combating cytotoxic stress. Elements of these cascades have been investigated in detail, but regulation of stress signal transduction from the cytoplasm to the nucleus is poorly understood. Herein are reported subcellular localization studies of fission yeast Spc1, a homolog of human p38 and budding yeast Hog1p SAPKs. Stress induces transient nuclear localization of Spc1. Nuclear translocation of Spc1 is coupled with disassociation from its activator kinase Wis1. However, Spc1 does not concentrate in the nucleus of δwis1 cells; therefore Wis1 does not tether Spc1 in the cytoplasm. Unphosphorylatable forms of Spc1 are dispersed in the cytoplasm and nucleus, even in cells that also produce wild-type Spc1. Thus, Spc1 must be phosphorylated by Wis1 to localize in the nucleus. Nuclear retention of Spc1 requires Atf1, a transcription factor that is the key nuclear substrate of Spc1. Nuclear localization of Atf1 requires Pcr1, a heterodimerization partner of Atf1. These studies show that phosphorylation and association with Atf1 are required for nuclear localization of Spc1.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1464-1473 |
| Number of pages | 10 |
| Journal | Genes and Development |
| Volume | 12 |
| Issue number | 10 |
| State | Published - May 15 1998 |
Fingerprint
Keywords
- Atf1
- Fission yeast
- Nuclear localization
- Schizosaccharomyces pombe
- Spc1
- Stress-activated protein kinase
ASJC Scopus subject areas
- Genetics
- Developmental Biology
Cite this
Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast. / Gaits, Frédérique; Degols, Geneviève; Shiozaki, Kazuhiro; Russell, Paul.
In: Genes and Development, Vol. 12, No. 10, 15.05.1998, p. 1464-1473.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast
AU - Gaits, Frédérique
AU - Degols, Geneviève
AU - Shiozaki, Kazuhiro
AU - Russell, Paul
PY - 1998/5/15
Y1 - 1998/5/15
N2 - Control of gene expression by stress-activated protein kinase (SAPK) cascades is crucial for combating cytotoxic stress. Elements of these cascades have been investigated in detail, but regulation of stress signal transduction from the cytoplasm to the nucleus is poorly understood. Herein are reported subcellular localization studies of fission yeast Spc1, a homolog of human p38 and budding yeast Hog1p SAPKs. Stress induces transient nuclear localization of Spc1. Nuclear translocation of Spc1 is coupled with disassociation from its activator kinase Wis1. However, Spc1 does not concentrate in the nucleus of δwis1 cells; therefore Wis1 does not tether Spc1 in the cytoplasm. Unphosphorylatable forms of Spc1 are dispersed in the cytoplasm and nucleus, even in cells that also produce wild-type Spc1. Thus, Spc1 must be phosphorylated by Wis1 to localize in the nucleus. Nuclear retention of Spc1 requires Atf1, a transcription factor that is the key nuclear substrate of Spc1. Nuclear localization of Atf1 requires Pcr1, a heterodimerization partner of Atf1. These studies show that phosphorylation and association with Atf1 are required for nuclear localization of Spc1.
AB - Control of gene expression by stress-activated protein kinase (SAPK) cascades is crucial for combating cytotoxic stress. Elements of these cascades have been investigated in detail, but regulation of stress signal transduction from the cytoplasm to the nucleus is poorly understood. Herein are reported subcellular localization studies of fission yeast Spc1, a homolog of human p38 and budding yeast Hog1p SAPKs. Stress induces transient nuclear localization of Spc1. Nuclear translocation of Spc1 is coupled with disassociation from its activator kinase Wis1. However, Spc1 does not concentrate in the nucleus of δwis1 cells; therefore Wis1 does not tether Spc1 in the cytoplasm. Unphosphorylatable forms of Spc1 are dispersed in the cytoplasm and nucleus, even in cells that also produce wild-type Spc1. Thus, Spc1 must be phosphorylated by Wis1 to localize in the nucleus. Nuclear retention of Spc1 requires Atf1, a transcription factor that is the key nuclear substrate of Spc1. Nuclear localization of Atf1 requires Pcr1, a heterodimerization partner of Atf1. These studies show that phosphorylation and association with Atf1 are required for nuclear localization of Spc1.
KW - Atf1
KW - Fission yeast
KW - Nuclear localization
KW - Schizosaccharomyces pombe
KW - Spc1
KW - Stress-activated protein kinase
UR - http://www.scopus.com/inward/record.url?scp=0032524018&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032524018&partnerID=8YFLogxK
M3 - Article
C2 - 9585506
AN - SCOPUS:0032524018
VL - 12
SP - 1464
EP - 1473
JO - Genes and Development
JF - Genes and Development
SN - 0890-9369
IS - 10
ER -