Disease relevance of TFEC

• TFEC is a transcriptional repressor originally identified in rat chondrosarcoma and contains a basic helix-loop-helix and leucine zipper (bHLH/LZ) structure [1].

High impact information on TFEC

• No TFEC RNA was detectable in several cell lines, including fibroblasts, myoblasts, chondrosarcoma cells, and myeloma cells, indicating that TFEC is not ubiquitously expressed [2].
• Cotransfection of TFEC DNA and TFE3 DNA strongly inhibits the transactivation caused by TFE3 [2].
• Like the in vitro translation product of TFE3, the in vitro-translated TFEC binds to the mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer [2].
• In contrast to TFE3, TFEC is unable to transactivate a reporter gene linked to a promoter containing tandem copies of the immunoglobulin mu E3 enhancer motif [2].
• The role of the closely related factors TFE3 and TFEC in MITF action was studied [3].

Biological context of TFEC

• TFECL contains an acidic domain that corresponds to a transcriptional activation domain of TFE3 but its equivalent region is deleted in rat TFEC [1].
• Furthermore, we observed that a considerable proportion of the TFEC transcripts splice out protein-coding exons, resulting in transcription factor isoforms lacking one or more functional domains, primarily the basic region and/or the AAD [4].
• In transient transfection assays, TFE3 and TFEC could collaborate with MITF to superactivate the tartrate resistant acid phosphatase (TRAP) promoter, a target for MITF in osteoclasts [3].
• The extracellular release of TFECP from T. foetus suggests that it is a potential virulence factor in bovine trichomoniasis [5].

Anatomical context of TFEC

• A novel TFEC transcript (TFEC-C) encodes an N-terminally truncated TFEC isoform lacking the acidic activation domain (AAD), and is exclusively expressed in kidney and small intestine [4].
• These results indicate that although different isoforms of MITF appear to be functionally similar, the TFE3 and TFEC proteins may collaborate with MITF to efficiently regulate expression of target genes in osteoclasts [3].

Associations of TFEC with chemical compounds

• These results indicate that this enzyme (TFECP) is a distinct cysteine proteinase [5].
• Bacitracin-purified T. foetus extracellular cysteine proteinase (TFECP) was separated in a denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel, electroblotted, and a 31-kDa band cut out for amino acid sequencing [5].

Other interactions of TFEC

• Furthermore, cDNA cloning by polymerase chain reaction yielded cDNAs for two TFEC isoforms, designated TFEC-l and TFEC-s, which are generated by alternative pre-mRNA splicing [6].
• We found that, similar to the MiTF gene, the genes for TFEB and TFEC contain multiple alternative first exons with restricted and differential tissue distributions [4].

Analytical, diagnostic and therapeutic context of TFEC

• Molecular cloning of cDNA encoding a human TFEC isoform, a newly identified transcriptional regulator [1].

References