ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism.

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Research Abstract Details 

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ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Abstract Text:

James E Ferguson,Yaxu Wu,Kevin Smith,Peter Charles,Kyle Powers,Hong Wang,Cam Patterson,

The molecular mechanisms of endothelial differentiation into a functional vascular network are incompletely understood. To identify novel factors in endothelial development, we used a microarray screen with differentiating embryonic stem (ES) cells that identified the gene for ankyrin repeat and SOCS box protein 4 (ASB4) as the most highly differentially expressed gene in the vascular lineage during early differentiation. Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). High levels of ASB4 expression in the embryonic vasculature coincide with drastic increases in oxygen tension as placental blood flow is initiated. However, as vessels mature and oxygen levels stabilize, ASB4 expression is quickly downregulated, suggesting that ASB4 may function to modulate an endothelium-specific response to increasing oxygen tension. Consistent with the hypothesis that ASB4 function is regulated by oxygen concentration, ASB4 interacts with the factor inhibiting HIF1alpha (FIH) and is a substrate for FIH-mediated hydroxylation via an oxygen-dependent mechanism. Additionally, overexpression of ASB4 in ES cells promotes differentiation into the vascular lineage in an oxygen-dependent manner. We postulate that hydroxylation of ASB4 in normoxia promotes binding to and degradation of substrate protein(s) to modulate vascular differentiation.

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Publishing Authors By Initials

JE Ferguson,Y Wu,K Smith,P Charles,K Powers,H Wang,C Patterson,

For similar investigative techniques: genetic techniques: cloning, molecular: two-hybrid system techniques research abstracts see: investigative techniques: genetic techniques: cloning, molecular: two-hybrid system techniques research

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ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular and cellular biology

VOLUME: 27

Page Numbers: 6407-19

Journal Abbreviation: Mol. Cell. Biol.

ISSN: 0270-7306

DAY: 16

MONTH: 07

YEAR: 2007

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Information

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LANGUAGE: eng

NlmUniqueID: 8109087

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Keywords Mesh Terms:

KEYWORDS: Two-Hybrid System Techniques

MESH TERMS: metabolism

Chemical & Substance for Abstract: ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Information

Substance Name: Oxygen

Registry Number: 7782-44-7

Grant and Affiliation Information for ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism.

AFFILIATION: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: HL 61656

ACRONYM: HL

MEDLINETA: Mol Cell Biol

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