Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Regulation of protein kinase CKII by direct interaction with the C-terminal region of p47(phox)
Autore:
Kim, YS; Lee, JH; Park, JW; Bae, YS;
Indirizzi:
Kyungpook Natl Univ, Coll Nat Sci, Dept Biochem, Taegu 702701, South KoreaKyungpook Natl Univ Taegu South Korea 702701 , Taegu 702701, South Korea
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 286, anno: 2001,
pagine: 87 - 93
SICI:
0006-291X(20010810)286:1<87:ROPKCB>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESPIRATORY BURST OXIDASE; GTP-BINDING PROTEIN; BETA-SUBUNIT; NADPH OXIDASE; CASEIN KINASE-2; SACCHAROMYCES-CEREVISIAE; CONFORMATIONAL-CHANGES; CYTOSOLIC COMPONENTS; CELLULAR-REGULATION; HUMAN-NEUTROPHILS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Bae, YS Kyungpook Natl Univ, Coll Nat Sci, Dept Biochem, Taegu 702701, South Korea Kyungpook Natl Univ Taegu South Korea 702701 702701, South Korea
Citazione:
Y.S. Kim et al., "Regulation of protein kinase CKII by direct interaction with the C-terminal region of p47(phox)", BIOC BIOP R, 286(1), 2001, pp. 87-93

Abstract

Protein kinase CKII is a Ser/Thr kinase which is involved in many proliferation-related processes in the cell. P47(phox) is a component of the leukocyte NADPH oxidase, which is an important element of host defense against microbial infection. In this study, we demonstrate that a truncated form of the p47(phox) lacking its N-terminal region (p47(phox)/SH3-C), but not a truncated form of the P47(phox) lacking its C-terminal region (p47 (phox)/N-SH3), undergoes better phosphorylation by CKII in the presence of arachidonicacid. The yeast two-hybrid test and the glutathione S-transferase (GST) pull-down assay showed that p47(phox) interacts specifically with the regulatory beta subunit (CKII beta), but not with the catalytic a subunit (CKII alpha) of the tetrameric CKII holoenzyme. The binding of p47(phox) to CKII beta requires the C-terminal region of p47(phox) and is completely abolished by addition of spermine, indicating that a highly basic region in the C-terminal region of p47(phox) contributes to binding to CKII beta. In addition,p47(phox) stimulates the catalytic activity of CKII holoenzyme; this stimulation also requires the C-terminal region of p47. Coimmunoprecipitation experiments showed that CKII holoenzyme interacts with p47(phox) in human neutrophils. Taken together, the present data indicate that the C-terminal region of p47 ph,, plays a significant role in the arachidonic acid-dependent phosphorylation of p47(phox) by CKII and that the same region of p47(phox) associates directly with CKII beta and can modulate the catalytic activity of CKII holoenzyme. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 18:55:25