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Publication : A new long form of c-Maf cooperates with Sox9 to activate the type II collagen gene.

First Author  Huang W Year  2002
Journal  J Biol Chem Volume  277
Issue  52 Pages  50668-75
PubMed ID  12381733 Mgi Jnum  J:80979
Mgi Id  MGI:2447911 Doi  10.1074/jbc.M206544200
Citation  Huang W, et al. (2002) A New Long Form of c-Maf Cooperates with Sox9 to Activate the Type II Collagen Gene. J Biol Chem 277(52):50668-75
abstractText  A new long form of the c-Maf transcription factor (Lc-Maf) was identified and shown to interact specifically with SOX9 in a yeast two-hybrid cDNA library screening. Lc-Maf encodes an extra 10 amino acids at the carboxyl terminus of c-Maf and contains a different 3'-untranslated region compared with c-Maf. The interaction between SOX9 and Lc-Maf was further confirmed by co-immunoprecipitation and glutathione S-transferase pull-down assays, which mapped the interacting domain of SOX9 to the high mobility group box DNA binding domain and that of Lc-Maf to the basic leucine zipper motif. In situ hybridizations showed that Lc-Maf RNA was coexpressed with Sox9 and Col2a1 RNA in areas of precartilaginous mesenchymal condensations during mouse embryo development. A DNA binding site of Lc-Maf was identified at the 5'-end of a 48-bp Col2a1 enhancer element near the high mobility group binding site of SOX9. Lc-Maf and SOX9 synergistically activated a luciferase reporter plasmid containing a Col2a1 enhancer and increased the transcription of the endogenous Col2a1 gene. In summary, Lc-Maf is the first transcription factor shown to interact with Sox9, to be coexpressed with Sox9 during an early step of chondrogenesis and to cooperate with Sox9 in activating a downstream target gene of Sox9.
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