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Article

The LRP5 high-bone-mass G171V mutation disrupts LRP5 interaction with Mesd.

Molecular and cellular biology - 1 Jun 2004

Zhang Yazhou, Wang Yang, Li Xiaofeng, Zhang Jianhong, Mao Junhao, Li Zhong, Zheng Jie, Li Lin, Harris Steve, Wu Dianqing

Abstract excerpt

The mechanism by which the high-bone-mass (HBM) mutation (G171V) of the Wnt coreceptor LRP5 regulates canonical Wnt signaling was investigated. The mutation was previously shown to reduce DKK1-mediated antagonism, suggesting that the first YWTD repeat domain where G171 is located may be responsible for DKK-mediated antagonism. However, we found that the third YWTD repeat, but not the first repeat domain, is...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 15143163
DOI: 10.1128/MCB.24.11.4677-4684.2004
PMCID: PMC416395

Genes

LRP5
DKK1
HBM

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The LRP5 high-bone-mass G171V mutation disrupts LRP5 interaction with Mesd.PMID 15143163Read ↗

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The WNT1G177C mutation specifically affects skeletal integrity in a mouse model of osteogenesis imperfecta type XVSemantic proximity Read ↗

High Bone Mass in Mice Expressing a Mutant <i>LRP5</i> GeneSemantic proximity Read ↗

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