PMID- 10398585
OWN - NLM
STAT- MEDLINE
DCOM- 19990813
LR  - 20161124
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 290
IP  - 4
DP  - 1999 Jul 23
TI  - Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein
      kinase CKII in vitro.
PG  - 839-50
AB  - IkappaBalpha is an inherently unstable protein which binds to and retains the
      ubiquitous transcription factor NFkappaB in the cytoplasm of resting cells. A
      continuous low level translocation of NFkappaB to the nucleus, secondary to the
      basal turnover of IkappaBalpha, is hypothesized to be necessary for cellular
      maturation, survival and, potentially, transformation. In response to cellular
      stimulation by inflammatory cytokines or mitogens, IkappaBalpha is rapidly
      degraded allowing larger pools of NFkappaB to translocate to the nucleus.
      Phosphorylation of IkappaBalpha at serine 32 (S32) and serine 36 (S36) is
      necessary for this stimuli-induced degradation. IKKalpha/beta kinases and
      p90(rsk1)are involved in stimuli-induced targeting of one or both of these
      IkappaBalpha sites. Whether other kinases phosphorylate S32 and S36 directly, and
      if so, what function they serve in NFkappaB activation remains unknown. Here we
      present evidence of a direct phosphorylation of IkappaBalpha at both S32 and S36 
      by purified or immunoprecipitated protein kinase CKII (PK-CKII) and a specific in
      vivo association between IkappaBalpha and PK-CKII. This PK-CKII-specific kinase
      activity is not found within the IKKalpha/beta-containing signalsome complex and 
      is biochemically distinct from that of the IKKalpha/beta kinases. The
      identification of an additional N-terminal IkappaBalpha kinase which is
      constitutively active and not significantly inducible raises numerous
      possibilities as to its role in cellular function.
CI  - Copyright 1999 Academic Press.
FAU - Taylor, J A
AU  - Taylor JA
AD  - Department of Immunology, Division of Infectious Diseases, Mayo Clinic,Rochester,
      MN 55905, USA.
FAU - Bren, G D
AU  - Bren GD
FAU - Pennington, K N
AU  - Pennington KN
FAU - Trushin, S A
AU  - Trushin SA
FAU - Asin, S
AU  - Asin S
FAU - Paya, C V
AU  - Paya CV
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (I-kappa B Proteins)
RN  - 0 (NFKBIA protein, human)
RN  - 0 (Nfkbia protein, rat)
RN  - 138-81-8 (2,3-Diphosphoglycerate)
RN  - 139874-52-5 (NF-KappaB Inhibitor alpha)
RN  - 452VLY9402 (Serine)
RN  - 9005-49-6 (Heparin)
RN  - EC 2.7.11.1 (Casein Kinase II)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.10 (CHUK protein, human)
RN  - EC 2.7.11.10 (I-kappa B Kinase)
RN  - EC 2.7.11.10 (IKBKB protein, human)
RN  - EC 2.7.11.10 (IKBKE protein, human)
RN  - EC 2.7.11.13 (Protein Kinase C)
SB  - IM
MH  - 2,3-Diphosphoglycerate/pharmacology
MH  - Animals
MH  - Casein Kinase II
MH  - DNA-Binding Proteins/*metabolism
MH  - Heparin/pharmacology
MH  - Humans
MH  - I-kappa B Kinase
MH  - *I-kappa B Proteins
MH  - NF-KappaB Inhibitor alpha
MH  - Phosphorylation
MH  - Precipitin Tests
MH  - Protein Kinase C/pharmacology
MH  - Protein-Serine-Threonine Kinases/*metabolism
MH  - Rats
MH  - Serine/*physiology
MH  - U937 Cells
EDAT- 1999/07/10 00:00
MHDA- 1999/07/10 00:01
CRDT- 1999/07/10 00:00
PHST- 1999/07/10 00:00 [pubmed]
PHST- 1999/07/10 00:01 [medline]
PHST- 1999/07/10 00:00 [entrez]
AID - 10.1006/jmbi.1999.2912 [doi]
AID - S0022-2836(99)92912-1 [pii]
PST - ppublish
SO  - J Mol Biol. 1999 Jul 23;290(4):839-50. doi: 10.1006/jmbi.1999.2912.