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Signal transduction of TGF-beta superfamily members is regulated by Smad proteins. In particular, Smads influence specific gene transcription by relaying signals from the cell membrane to the nucleus. Smad4 plays an essential role in TGF-beta-induced transcriptional activation wherein phosphorylated receptor-associated Smads associate with Smad4. Furthermore, SMIF (Smad4-intereacting protein) and Smad4 complex with TGF-beta and BMP4. An increase in Smad4 concentration increases the translocation of this complex to the nucleus. SMIF and Smad4 interact directly through a EVH1/WH1 domain on SMIF and a proline-rich activation domain on Smad4. Smad4 is essential to nuclear translocation of SMIF as deletion of the Smad4-interacting domain (located in the N-terminal 100 amino acids) of SMIF eliminates TGF-beta-induced nuclear translocation of SMIF. The human SMIF gene is ubiquitously expressed and encodes a protein with a relative molecular mass of 70 kDa.
1110066A22Rik; 4930568L04Rik; AU019772; D14Ertd817e; DCP1 decapping enzyme homolog A; DCP1 decapping enzyme homolog A (S. cerevisiae); DCP1 decapping enzyme-like protein A; DCP1A; decapping enzyme; decapping enzyme hDcp1a; decapping mRNA 1A; FLJ21691; HSA275986; MAD homolog 4 interacting transcription coactivator 1; MAD homolog 4-interacting transcription coactivator 1; Mitc1; mRNA-decapping enzyme 1A; Nbla00360; putative protein product of Nbla00360; RGD1561298; Smad4-interacting transcriptional co-activator; SMAD4IP1; SMIF; test2; transcription factor SMIF
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