In:
Science, American Association for the Advancement of Science (AAAS), Vol. 284, No. 5412 ( 1999-04-09), p. 309-313
Abstract:
IκB [inhibitor of nuclear factor κB (NF-κB)] kinase (IKK) phosphorylates IκB inhibitory proteins, causing their degradation and activation of transcription factor NF-κB, a master activator of inflammatory responses. IKK is composed of three subunits—IKKα and IKKβ, which are highly similar protein kinases, and IKKγ, a regulatory subunit. In mammalian cells, phosphorylation of two sites at the activation loop of IKKβ was essential for activation of IKK by tumor necrosis factor and interleukin-1. Elimination of equivalent sites in IKKα, however, did not interfere with IKK activation. Thus, IKKβ, not IKKα, is the target for proinflammatory stimuli. Once activated, IKKβ autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.284.5412.309
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
1999
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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