Abstract
A precursor, p105, for one of the subunits (p50) of the NF-κB transcription factor, plays an important role in inducible expression of diverse cellular genes, p105 also functions as a cytoplasmic inhibitor for NF-κB, and the proteolytic processing of its inhibitory C-terminal region is required for generation of active NF-κB. Here, it is reported that the human p105 C-terminal region is phosphorylated in vivo on Ser894 and Ser908, which are potential phosphorylation sites in vitro for proline-directed serine/threonine kinases such as cyclin-dependent kinase. Furthermore, the mutation of these in vivo phosphorylation sites retards p105 processing in vivo, suggesting that p105 processing is regulated in a phosphorylation-dependent manner.
| Original language | English |
|---|---|
| Pages (from-to) | 183-189 |
| Number of pages | 7 |
| Journal | Gene |
| Volume | 165 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1995 |
| Externally published | Yes |
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Keywords
- inflammation
- p105
- proteasome
- Transcription factor
ASJC Scopus subject areas
- Genetics
Cite this
A role for phosphorylation in the proteolytic processing of the human NF-KB1 precursor. / Fujimoto, Koutarou; Yasuda, Hideyo; Sato, Yoshihisa; Yamamoto, Ken-ichi.
In: Gene, Vol. 165, No. 2, 1995, p. 183-189.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A role for phosphorylation in the proteolytic processing of the human NF-KB1 precursor
AU - Fujimoto, Koutarou
AU - Yasuda, Hideyo
AU - Sato, Yoshihisa
AU - Yamamoto, Ken-ichi
PY - 1995
Y1 - 1995
N2 - A precursor, p105, for one of the subunits (p50) of the NF-κB transcription factor, plays an important role in inducible expression of diverse cellular genes, p105 also functions as a cytoplasmic inhibitor for NF-κB, and the proteolytic processing of its inhibitory C-terminal region is required for generation of active NF-κB. Here, it is reported that the human p105 C-terminal region is phosphorylated in vivo on Ser894 and Ser908, which are potential phosphorylation sites in vitro for proline-directed serine/threonine kinases such as cyclin-dependent kinase. Furthermore, the mutation of these in vivo phosphorylation sites retards p105 processing in vivo, suggesting that p105 processing is regulated in a phosphorylation-dependent manner.
AB - A precursor, p105, for one of the subunits (p50) of the NF-κB transcription factor, plays an important role in inducible expression of diverse cellular genes, p105 also functions as a cytoplasmic inhibitor for NF-κB, and the proteolytic processing of its inhibitory C-terminal region is required for generation of active NF-κB. Here, it is reported that the human p105 C-terminal region is phosphorylated in vivo on Ser894 and Ser908, which are potential phosphorylation sites in vitro for proline-directed serine/threonine kinases such as cyclin-dependent kinase. Furthermore, the mutation of these in vivo phosphorylation sites retards p105 processing in vivo, suggesting that p105 processing is regulated in a phosphorylation-dependent manner.
KW - inflammation
KW - p105
KW - proteasome
KW - Transcription factor
UR - http://www.scopus.com/inward/record.url?scp=0028839703&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028839703&partnerID=8YFLogxK
U2 - 10.1016/0378-1119(95)00507-3
DO - 10.1016/0378-1119(95)00507-3
M3 - Article
C2 - 8522173
AN - SCOPUS:0028839703
VL - 165
SP - 183
EP - 189
JO - Gene
JF - Gene
SN - 0378-1119
IS - 2
ER -