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MafA transcription factor is phosphorylated by p38 MAP kinase
- Source :
- FEBS letters. 579(17)
- Publication Year :
- 2005
-
Abstract
- Basic-leucine zipper transcription factors of the Maf family are key regulators of various developmental and differentiation processes. We previously reported that the phosphorylation status of MafA is a critical determinant of its biological functions. Using Western blot and mass spectrometry analysis, we now show that MafA is phosphorylated by p38 MAP kinase and identify three phosphoacceptor sites: threonine 113 and threonine 57, evolutionarily conserved residues located in the transcription activating domain, and serine 272. Mutation of these residues severely impaired MafA biological activity. Furthermore, we show that p38 also phosphorylates MafB and c-Maf. Together, these findings suggest that the p38 MAP kinase pathway is a novel regulator of large Maf transcription factors.
- Subjects :
- Threonine
Molecular Sequence Data
Biophysics
Basic helix-loop-helix leucine zipper transcription factors
Biology
Biochemistry
Quail
p38 Mitogen-Activated Protein Kinases
Lens
Mice
Structural Biology
Transcription (biology)
Maf Transcription Factors
Proto-Oncogene Proteins
Lens, Crystalline
Genetics
Serine
Animals
Humans
Amino Acid Sequence
Phosphorylation
AP1
Molecular Biology
Transcription factor
MAPK14
Cell Differentiation
Cell Biology
Maf
MAPK
DNA-Binding Proteins
AP-1 transcription factor
MAFB
Mitogen-activated protein kinase
Proto-Oncogene Proteins c-maf
Mutation
biology.protein
Nrl
Kreisler
Chickens
Transcription Factors
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 579
- Issue :
- 17
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....828368c9c1a8a3cc32c4c13df72bfe19