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J Biochem. 2009 Feb;145(2):129-35. doi: 10.1093/jb/mvn158. Epub 2008 Nov 23.

TAL1/SCL relieves the E2-2-mediated repression of VEGFR2 promoter activity.

Author information

1
Department of Experimental Pathology, Graduate School of Comprehensive Human Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8575, Japan.

Abstract

The basic helix-loop-helix (bHLH) protein TAL1/SCL is essential for embryonic-vascular development. TAL1/SCL regulates the activation of endothelial cells by binding directly or indirectly to DNA sequences in critical target genes. We recently demonstrated that E-box protein E2-2 blocks endothelial cell activation via perturbation of VEGFR2 promoter activity. Herein, we report that TAL1/SCL interacts with E2-2 and inhibits E2-2-mediated effects on reporter activity. Mutational analysis revealed that the HLH domain of TAL1/SCL, but not its basic region, is required for interaction with E2-2. Importantly, TAL1/SCL relieves the E2-2-mediated repression of VEGFR2 reporter activity in endothelial cells. Our data elaborate on the bHLH protein interactions that regulate endothelial cell activation.

PMID:
19029143
DOI:
10.1093/jb/mvn158
[Indexed for MEDLINE]

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