Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha.
Hypoxia inducible factor-1 alpha (HIF-1 alpha) is a central component of the cellular responses to hypoxia. Hypoxic conditions result in stabilization of HIF-1 alpha and formation of the transcriptionally active HIF-1 complex. It was suggested that mammalian ARD1 acetylates HIF-1 alpha and thereby enhances HIF-1 alpha ubiquitination and degradation. Furthermore, ARD1 was proposed to be down-regulated in hypoxia thus facilitating the stabilization of HIF-1 alpha. Here we demonstrate that the level of human ARD1 (hARD1) protein is not decreased in hypoxia. Moreover, hARD1 does not acetylate and destabilize HIF-1 alpha. However, we find that hARD1 specifically binds HIF-1 alpha, suggesting a putative, still unclear, connection between these proteins.
Arnesen
Thomas
T
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Kong
Xianguo
X
Evjenth
Rune
R
Gromyko
Darina
D
Varhaug
Jan Erik
JE
Lin
Zhao
Z
Sang
Nianli
N
Caro
Jaime
J
Lillehaug
Johan R
JR
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000693:Anaerobiosis; D002478:Cells, Cultured; D006801:Humans; D051795:Hypoxia-Inducible Factor 1, alpha Subunit / Q000378:metabolism*; D063209:N-Terminal Acetyltransferase A; D063213:N-Terminal Acetyltransferase E
C497442:HIF1A protein, human; D051795:Hypoxia-Inducible Factor 1, alpha Subunit; D000123:Acetyltransferases; D063209:N-Terminal Acetyltransferase A; C504824:NAA10 protein, human; D063213:N-Terminal Acetyltransferase E