The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis.

A mutants of p47phox. The mutant containing S-->A mutations involving all serines between S303 and S379 [S(303-379)A] was not phosphorylated, did not translocate to plasma membrane during activation and was almost devoid of function. As to individual serines, S379 was of special interest because (a) p47 phox S379 was phosphorylated in phorbol-activated lymphoblasts expressing wild-type p47phox, and (b) p47phox S379A failed to translocate to the membrane, and was as functionless as p47phox S(303-379)A; other single S-->A mutations had little effect on oxidase activity. These findings suggest that the phosphorylation of S379 may be important for oxidase activation in whole cells. -->
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Grant Information: AI-24227 United States AI NIAID NIH HHS; AI-28479 United States AI NIAID NIH HHS; RR-00833 United States RR NCRR NIH HHS
Substance Nomenclature: 0 (Oligonucleotides, Antisense)
0 (Phosphoproteins)
0 (Recombinant Proteins)
452VLY9402 (Serine)
EC 1.6.- (NADH, NADPH Oxidoreductases)
EC 1.6.3.- (NADPH Oxidases)
EC 1.6.3.1 (neutrophil cytosolic factor 1)
EC 1.6.99.- (superoxide-forming enzyme)
EC 1.6.99.1 (NADPH Dehydrogenase)
Entry Date(s): Date Created: 19950901 Date Completed: 19951004 Latest Revision: 20181113
Update Code: 20231215
PubMed Central ID: PMC185774
DOI: 10.1172/JCI118187
PMID: 7657821
Autor: Faust LR; Scripps Research Institute, La Jolla, California 92037, USA., el Benna J, Babior BM, Chanock SJ
Jazyk: angličtina
Zdroj: The Journal of clinical investigation [J Clin Invest] 1995 Sep; Vol. 96 (3), pp. 1499-505.
DOI: 10.1172/JCI118187
Abstrakt: The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of oxygen to O2- at the expense of NADPH. Dormant in resting cells, the oxidase is activated by exposing the cells to appropriate stimuli. During activation, p47phox, a cytosolic oxidase subunit, becomes extensively phosphorylated on a number of serines located between S303 and S379. To determine whether this phosphorylation is necessary for oxidase activation, we examined phorbol-elicited oxidase activity in EBV-transformed B lymphoblasts deficient in p47phox after transfection with plasmids expressing various S-->A mutants of p47phox. The mutant containing S-->A mutations involving all serines between S303 and S379 [S(303-379)A] was not phosphorylated, did not translocate to plasma membrane during activation and was almost devoid of function. As to individual serines, S379 was of special interest because (a) p47 phox S379 was phosphorylated in phorbol-activated lymphoblasts expressing wild-type p47phox, and (b) p47phox S379A failed to translocate to the membrane, and was as functionless as p47phox S(303-379)A; other single S-->A mutations had little effect on oxidase activity. These findings suggest that the phosphorylation of S379 may be important for oxidase activation in whole cells.
Databáze: MEDLINE
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