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Abstract


Egr-I is a zinc finger transcription factor and one of immediate early response genes. Egr-l is upregulated in response to a wide variety of mitogenic and nonmitogenic stimuli, including peptide growth factors, shear stress, urea, hypotonicity and hypoxia. To identify novel Egr-l interacting protein, we performed yeast two-hybrid screening using Egr-l baits. In this study, we identified that proteasome subunit ¥átype 3 (PSMA3) and protein inhibitor of activated STAT protein (PIASy) interacts specifically with Egr-l protein by yeast two-hybrid screening. In addition, we found that the stability of Egr-l was increased under hypoxic condition. these results suggested the importance of £Ï©ütension in the degradation processes of Egr-l.

Å°¿öµå

Egr-1; Two-hybrid; Proteasome subunit ¥á type 3; ProtehI inhibitor of activated STAT protein y; Hypoxia

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