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Details on Person Based on electrophoretic mobility shift assays conducted wit...
| Class:Id | Summation:9857344 |
|---|---|
| _displayName | Based on electrophoretic mobility shift assays conducted wit... |
| _timestamp | 2024-04-04 16:23:11 |
| created | [InstanceEdit:9857351] Rothfels, Karen, 2024-01-04 |
| modified | [InstanceEdit:9857592] Rothfels, Karen, 2024-01-07 [InstanceEdit:9863222] Rothfels, Karen, 2024-02-28 [InstanceEdit:9863506] Rothfels, Karen, 2024-03-01 [InstanceEdit:9907117] Rothfels, Karen, 2024-04-04 |
| text | Based on electrophoretic mobility shift assays conducted with mouse proteins, MITF dimerizes with itself or any of the related MiT family member transcription factors TFE3, TFEB and TFEC (Hemesath et al, 1994; Fisher et al, 1991; Zhao et al, 1993), but not with other BHLH or BHLH-Zip transcription factors. Dimerization appears to be required for DNA binding, and there is some evidence that in the absence of DNA, the transcription factors may form tetrameric complexes (Fisher et al, 1991). DNA is contacted in the major groove by the basic domain of MITF (Hemesath et al, 1994; Pogenberg et al, 2012; reviewed by Goding and Arnheiter, 2019). TFEC shows more restricted expression than other members of the MiT family, while TFEB, TFE3 and some MITF isoforms are widely expressed (Hemesath et al, 1994; Rehli et al 199; Kuiper et al, 2004). Despite the ability of each of their encoded proteins to form heterodimers with MITF, knockouts of TFE3, TFEB and TFEC do not affect melanocyte development, suggesting that only MITF homodimers are essential for this role (Steingrimsson et al, 2002; reviewed in Hou and Pavan, 2008; Goding and Arnheiter, 2019) |
| (summation) | [Reaction:9857375] MITF dimerizes [Homo sapiens] |
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