Abstract
The basic helix–loop–helix protein E2-2 is known to play a role in quiescence of endothelial cells (ECs). However, it is unclear how the activity of E2-2 is controlled in the cells. In this study, we identified FAM96B as an interaction partner of E2-2. FAM96B interfered with E2-2-mediated effects on luciferase reporter activities. Furthermore, the suppression of vascular endothelial growth factor receptor 2 promoter activity by E2-2 was rescued by the expression of FAM96B in a dose-dependent manner. Interestingly, FAM96B decreased the expression of ectopic and endogenous E2-2 proteins. Mutational analysis revealed that the middle region of FAM96B is required for the limited expression of E2-2 protein. When FAM96B was expressed in ECs, the EC migration, proliferation, and tube formation were potentiated. Taken together, these findings suggest that FAM96B acts as a regulator of E2-2 through the control of its protein expression.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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Basic Helix-Loop-Helix Transcription Factors / genetics
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Basic Helix-Loop-Helix Transcription Factors / metabolism
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COS Cells
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Movement
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Cell Proliferation
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Cricetinae
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Endothelial Cells / metabolism*
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Helix-Loop-Helix Motifs
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Humans
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Metalloproteins
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Mice
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NIH 3T3 Cells
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Promoter Regions, Genetic
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Sequence Analysis, DNA
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Transcription Factor 7-Like 2 Protein / genetics
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Transcription Factor 7-Like 2 Protein / metabolism*
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Vascular Endothelial Growth Factor Receptor-2 / genetics*
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Vascular Endothelial Growth Factor Receptor-2 / metabolism
Substances
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Basic Helix-Loop-Helix Transcription Factors
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CIAO2B protein, human
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Carrier Proteins
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Metalloproteins
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Nuclear Proteins
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TCF7L2 protein, human
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Transcription Factor 7-Like 2 Protein
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Vascular Endothelial Growth Factor Receptor-2