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The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.

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Authors
Foxler, Daniel E
Bridge, Katherine S
James, Victoria
Webb, Thomas M
Mee, Maureen
Wong, Sybil C K
Feng, Yunfeng
Constantin-Teodosiu, Dumitru
Petursdottir, Thorgunnur Eyfjord
Bjornsson, Johannes
Ingvarsson, Sigurdur
Ratcliffe, Peter J
Longmore, Gregory D
Sharp, Tyson V
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Issue Date
2012-02

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Citation
Nat. Cell Biol. 2012, 14(2):201-8
Abstract
There are three prolyl hydroxylases (PHD1, 2 and 3) that regulate the hypoxia-inducible factors (HIFs), the master transcriptional regulators that respond to changes in intracellular O(2) tension. In high O(2) tension (normoxia) the PHDs hydroxylate two conserved proline residues on HIF-1α, which leads to binding of the von Hippel-Lindau (VHL) tumour suppressor, the recognition component of a ubiquitin-ligase complex, initiating HIF-1α ubiquitylation and degradation. However, it is not known whether PHDs and VHL act separately to exert their enzymatic activities on HIF-1α or as a multiprotein complex. Here we show that the tumour suppressor protein LIMD1 (LIM domain-containing protein) acts as a molecular scaffold, simultaneously binding the PHDs and VHL, thereby assembling a PHD-LIMD1-VHL protein complex and creating an enzymatic niche that enables efficient degradation of HIF-1α. Depletion of endogenous LIMD1 increases HIF-1α levels and transcriptional activity in both normoxia and hypoxia. Conversely, LIMD1 expression downregulates HIF-1 transcriptional activity in a manner depending on PHD and 26S proteasome activities. LIMD1 family member proteins Ajuba and WTIP also bind to VHL and PHDs 1 and 3, indicating that these LIM domain-containing proteins represent a previously unrecognized group of hypoxic regulators.
Additional Links
http://www.nature.com/ncb/journal/v14/n2/full/ncb2424.html
http://dx.doi.org/10.1038/ncb2424
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Archived with thanks to Nature cell biology
ae974a485f413a2113503eed53cd6c53
10.1038/ncb2424
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