MITF dimerizes

Stable Identifier
R-HSA-9857375
Type
Reaction [binding]
Species
Homo sapiens
Compartment
nucleoplasm
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
MITF dimerizes
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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)
Literature References
PubMed ID Title Journal Year
11930005 Mitf and Tfe3, two members of the Mitf-Tfe family of bHLH-Zip transcription factors, have important but functionally redundant roles in osteoclast development

Steingrímsson, E, Tessarollo, L, Pathak, B, Hou, L, Arnheiter, H, Copeland, NG, Jenkins, NA

Proc Natl Acad Sci U S A 2002
19002157 Transcriptional and signaling regulation in neural crest stem cell-derived melanocyte development: do all roads lead to Mitf?

Hou, L, Pavan, WJ

Cell Res 2008
9973413 TFEC is a macrophage-restricted member of the microphthalmia-TFE subfamily of basic helix-loop-helix leucine zipper transcription factors

Rehli, M, Lichanska, A, Cassady, AI, Ostrowski, MC, Hume, DA

J Immunol 1999
15118077 Regulation of the MiTF/TFE bHLH-LZ transcription factors through restricted spatial expression and alternative splicing of functional domains

Kuiper, RP, Schepens, M, Thijssen, J, Schoenmakers, EF, van Kessel, AG

Nucleic Acids Res 2004
8336698 TFEC, a basic helix-loop-helix protein, forms heterodimers with TFE3 and inhibits TFE3-dependent transcription activation

Zhao, GQ, Zhao, Q, Zhou, X, Mattei, MG, de Crombrugghe, B

Mol Cell Biol 1993
7958932 microphthalmia, a critical factor in melanocyte development, defines a discrete transcription factor family

Hemesath, TJ, Steingrìmsson, E, McGill, G, Hansen, MJ, Vaught, J, Hodgkinson, CA, Arnheiter, H, Copeland, NG, Jenkins, NA, Fisher, DE

Genes Dev 1994
31123060 MITF-the first 25 years

Goding, CR, Arnheiter, H

Genes Dev 2019
1748288 TFEB has DNA-binding and oligomerization properties of a unique helix-loop-helix/leucine-zipper family

Fisher, DE, Carr, CS, Parent, LA, Sharp, PA

Genes Dev 1991
23207919 Restricted leucine zipper dimerization and specificity of DNA recognition of the melanocyte master regulator MITF

Pogenberg, V, Ogmundsdóttir, MH, Bergsteinsdóttir, K, Schepsky, A, Phung, B, Deineko, V, Milewski, M, Steingrímsson, E, Wilmanns, M

Genes Dev 2012
Participants
Input
Output
Participates
as an event of
Inferred From
MiT family members dimerize (Mus musculus)
Authored
Rothfels, K  (2023-12-21)
Reviewed
Arnheiter, H  (2024-02-26)
de la Serna, IL  (2024-05-21)
Vu, HN  (2024-11-05)
Steingrímsson, E  (2024-11-05)
Created
Rothfels, K  (2024-01-04)
Cite Us!