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TAZ: a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins.

The highly conserved and ubiquitously expressed 14-3-3 proteins regulate differentiation, cell cycle progression and apoptosis by binding intracellular phosphoproteins involved in signal transduction. By screening in vitro translated cDNA pools for the ability to bind 14-3-3, we identified a novel transcriptional co-activator, TAZ (transcriptional co-activator with PDZ-binding motif) as a 14-3-3-binding molecule. TAZ shares homology with Yes-associated protein (YAP), contains a WW domain and functions as a transcriptional co-activator by binding to the PPXY motif present on transcription factors. 14-3-3 binding requires TAZ phosphorylation on a single serine residue, resulting in the inhibition of TAZ transcriptional co-activation through 14-3-3-mediated nuclear export. The C-terminus of TAZ contains a highly conserved PDZ-binding motif that localizes TAZ into discrete nuclear foci and is essential for TAZ-stimulated gene transcription. TAZ uses this same motif to bind the PDZ domain-containing protein NHERF-2, a molecule that tethers plasma membrane ion channels and receptors to cytoskeletal actin. TAZ may link events at the plasma membrane and cytoskeleton to nuclear transcription in a manner that can be regulated by 14-3-3.

Pubmed ID: 11118213


  • Kanai F
  • Marignani PA
  • Sarbassova D
  • Yagi R
  • Hall RA
  • Donowitz M
  • Hisaminato A
  • Fujiwara T
  • Ito Y
  • Cantley LC
  • Yaffe MB


The EMBO journal

Publication Data

December 15, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM56203
  • Agency: NIGMS NIH HHS, Id: GM59281
  • Agency: NHLBI NIH HHS, Id: HL03601
  • Agency: NIGMS NIH HHS, Id: R01 GM056203

Mesh Terms

  • 14-3-3 Proteins
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Cell Line
  • Chickens
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Mice
  • Molecular Sequence Data
  • Phosphorylation
  • Proteins
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcription Factors
  • Tyrosine 3-Monooxygenase