Abstract:
:Alpha-catenin, an integral part of cadherin-catenin adhesion complexes, is a major binding partner of beta-catenin, a key component of the Wnt pathway, which activates T-cell factor (TCF)/lymphoid enhancer factor (LEF) transcription and is often upregulated in cancers. Recently, we identified an alpha-catenin-related protein, alpha-catulin, whose function is poorly understood, as part of a Rho GTPase signaling complex. Here, based on evidence suggesting that alpha-catulin may associate with a beta-catenin fraction, we investigated the role of alpha-catenin family members in beta-catenin-mediated signals. Expression of the full length or a 103-residue region of alpha-catenin strongly inhibits the induction of the TCF/LEF-responsive TOPFLASH reporter in HEK293T cells expressing activated beta-catenin or in cancer cells with constitutively upregulated Wnt signaling, whereas alpha-catulin expression had no effect. Interestingly, alpha-catulin expression attenuates the activation of the cyclin D1 promoter, a target of Wnt pathway signals. Alpha-catulin appears to inhibit Ras-mediated signals to the cyclin D1 promoter, rather than beta-catenin signals, and the synergy between Ras and beta-catenin required to fully activate this promoter. Data suggesting the involvement of Rho in this response are presented and discussed. These results suggest a novel function for alpha-catulin and imply that alpha-catenin and alpha-catulin have distinct activities that downregulate, respectively, beta-catenin and Ras signals converging on the cyclin D1 promoter.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Merdek KD,Nguyen NT,Toksoz Ddoi
10.1128/mcb.24.6.2410-2422.2004subject
Has Abstractpub_date
2004-03-01 00:00:00pages
2410-22issue
6eissn
0270-7306issn
1098-5549journal_volume
24pub_type
杂志文章abstract::Replication protein A (RPA) is required for simian virus 40-directed DNA replication in vitro and for nucleotide excision repair (NER). Here we report that RPA and the human repair protein XPA specifically interact both in vitro and in vivo. Mapping of the RPA-interactive domains in XPA revealed that both of the large...
journal_title:Molecular and cellular biology
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1984-09-01 00:00:00
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pub_type: 杂志文章
doi:10.1128/mcb.16.12.6851
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pub_type: 杂志文章
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更新日期:1981-04-01 00:00:00