Small Maf proteins (MafF, MafG, MafK): History, structure and function

Research output: Contribution to journalReview articlepeer-review

71 Citations (Scopus)

Abstract

The small Maf proteins (sMafs) are basic region leucine zipper (bZIP)-type transcription factors. The basic region of the Maf family is unique among the bZIP factors, and it contributes to the distinct DNA-binding mode of this class of proteins. MafF, MafG and MafK are the three vertebrate sMafs, and no functional differences have been observed among them in terms of their bZIP structures. sMafs form homodimers by themselves, and they form heterodimers with cap ‘n’ collar (CNC) proteins (p45 NF-E2, Nrf1, Nrf2, and Nrf3) and also with Bach proteins (Bach1 and Bach2). Because CNC and Bach proteins cannot bind to DNA as monomers, sMafs are indispensable partners that are required by CNC and Bach proteins to exert their functions. sMafs lack the transcriptional activation domain; hence, their homodimers act as transcriptional repressors. In contrast, sMafs participate in transcriptional activation or repression depending on their heterodimeric partner molecules and context. Mouse genetic analyses have revealed that various biological pathways are under the regulation of CNC-sMaf heterodimers. In this review, we summarize the history and current progress of sMaf studies in relation to their partners.

Original languageEnglish
Pages (from-to)197-205
Number of pages9
JournalGene
Volume586
Issue number2
DOIs
Publication statusPublished - 2016 Jul 25

Keywords

  • MafF
  • MafG
  • MafK
  • Small Maf
  • bZIP transcription factor

ASJC Scopus subject areas

  • Genetics

Fingerprint Dive into the research topics of 'Small Maf proteins (MafF, MafG, MafK): History, structure and function'. Together they form a unique fingerprint.

Cite this