PMID- 14643885
OWN - NLM
STAT- MEDLINE
DCOM- 20040805
LR  - 20220409
IS  - 1357-2725 (Print)
IS  - 1357-2725 (Linking)
VI  - 36
IP  - 2
DP  - 2004 Feb
TI  - The mammalian basic helix-loop-helix/PAS family of transcriptional regulators.
PG  - 189-204
AB  - Basic helix-loop-helix (bHLH)/PAS proteins are critical regulators of gene 
      expression networks underlying many essential physiological and developmental 
      processes. These include transcriptional responses to environmental pollutants 
      and low oxygen tension, mediated by the aryl hydrocarbon (Dioxin) receptor and 
      hypoxia inducible factors (HIF), respectively, and controlling aspects of neural 
      development, mediated by the single minded (SIM) proteins. bHLH proteins must 
      dimerise to form functional DNA binding complexes and bHLH/PAS proteins are 
      distinguished from other members of the broader bHLH superfamily by the 
      dimerisation specificity conferred by their PAS homology domains. bHLH/PAS 
      proteins tend to be ubiquitous, latent signal-regulated transcription factors 
      that often recognise variant forms of the classic E-box enhancer sequence bound 
      by other bHLH proteins. Two closely related forms of each of the hypoxia 
      inducible factors alpha and single minded proteins and the general partner 
      protein, aryl hydrocarbon receptor nuclear translocator (ARNT), are present in 
      many cell types. Despite high sequence conservation within their DNA binding and 
      dimerisation domains, and having very similar DNA recognition specificities, the 
      homologues are functionally non-redundant and biologically essential. While the 
      mechanisms controlling partner choice and target gene activation that determine 
      this functional specificity are poorly understood, interactions mediated by the 
      PAS domains are essential. Information on structures and protein/protein 
      interactions for members of the steroid hormone/nuclear receptor superfamily has 
      contributed to our understanding of the way these receptors function and assisted 
      the development of highly specific agonists and antagonists. Similarly, it is 
      anticipated that developing a detailed mechanistic and structural understanding 
      of bHLH/PAS proteins will ultimately facilitate drug design.
FAU - Kewley, Robyn J
AU  - Kewley RJ
AD  - School of Molecular and Biomedical Science (Biochemistry), University of 
      Adelaide, Adelaide, SA 5005, Australia.
FAU - Whitelaw, Murray L
AU  - Whitelaw ML
FAU - Chapman-Smith, Anne
AU  - Chapman-Smith A
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Netherlands
TA  - Int J Biochem Cell Biol
JT  - The international journal of biochemistry & cell biology
JID - 9508482
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Receptors, Aryl Hydrocarbon)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
SB  - IM
MH  - Animals
MH  - Cysteine Endopeptidases/metabolism
MH  - Drug Design
MH  - Gene Expression Regulation
MH  - *Helix-Loop-Helix Motifs
MH  - Humans
MH  - Models, Biological
MH  - Multienzyme Complexes/metabolism
MH  - Multigene Family
MH  - Neurons/metabolism
MH  - Proteasome Endopeptidase Complex
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Receptors, Aryl Hydrocarbon/chemistry/metabolism
MH  - Signal Transduction
MH  - *Transcription, Genetic
MH  - Transcriptional Activation
RF  - 100
EDAT- 2003/12/04 05:00
MHDA- 2004/08/06 05:00
CRDT- 2003/12/04 05:00
PHST- 2003/12/04 05:00 [pubmed]
PHST- 2004/08/06 05:00 [medline]
PHST- 2003/12/04 05:00 [entrez]
AID - S1357272503002115 [pii]
AID - 10.1016/s1357-2725(03)00211-5 [doi]
PST - ppublish
SO  - Int J Biochem Cell Biol. 2004 Feb;36(2):189-204. doi: 
      10.1016/s1357-2725(03)00211-5.