PMID- 38109992
OWN - NLM
STAT- MEDLINE
DCOM- 20240223
LR  - 20240315
IS  - 1089-8638 (Electronic)
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 436
IP  - 3
DP  - 2024 Feb 1
TI  - Dimerization Rules of Mammalian PAS Proteins.
PG  - 168406
LID - S0022-2836(23)00523-5 [pii]
LID - 10.1016/j.jmb.2023.168406 [doi]
AB  - The PAS (PER, ARNT, SIM) protein family plays a vital role in mammalian biology 
      and human disease. This analysis arose from an interest in the signaling 
      mechanics by the Ah receptor (AHR) and the Ah receptor nuclear translocator 
      (ARNT). After more than fifty years by studying this and related mammalian sensor 
      systems, describing the role of PAS domains in signal transduction is still 
      challenging. In this perspective, we attempt to interpret recent studies of 
      mammalian PAS protein structure and consider how this new insight might explain 
      how these domains are employed in human signal transduction with an eye towards 
      developing strategies to target and engineer these molecules for a new generation 
      of therapeutics. Our approach is to integrate our understanding of PAS protein 
      history, cell biology, and molecular biology with recent structural discoveries 
      to help explain the mechanics of mammalian PAS protein signaling. As a learning 
      set, we focus on sequences and crystal structures of mammalian PAS protein dimers 
      that can be visualized using readily available software.
CI  - Copyright (c) 2023. Published by Elsevier Ltd.
FAU - Rojas, Brenda L
AU  - Rojas BL
AD  - Molecular and Environmental Toxicology Center, University of Wisconsin at 
      Madison, USA.
FAU - Vazquez-Rivera, Emmanuel
AU  - Vazquez-Rivera E
AD  - Molecular and Environmental Toxicology Center, University of Wisconsin at 
      Madison, USA.
FAU - Partch, Carrie L
AU  - Partch CL
AD  - Department of Chemistry and Biochemistry, University of California at Santa Cruz, 
      USA.
FAU - Bradfield, Christopher A
AU  - Bradfield CA
AD  - Molecular and Environmental Toxicology Center, University of Wisconsin at 
      Madison, USA; McArdle Laboratory for Cancer Research. University of Wisconsin, 
      School of Medicine and Public Health, Madison, WI, USA. Electronic address: 
      bradfield@oncology.wisc.edu.
LA  - eng
GR  - R35 ES028377/ES/NIEHS NIH HHS/United States
GR  - P30 CA014520/CA/NCI NIH HHS/United States
GR  - R25 ES020720/ES/NIEHS NIH HHS/United States
GR  - R35 GM141849/GM/NIGMS NIH HHS/United States
GR  - T32 ES007015/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20231216
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 138391-32-9 (Aryl Hydrocarbon Receptor Nuclear Translocator)
RN  - 0 (Receptors, Aryl Hydrocarbon)
SB  - IM
MH  - Animals
MH  - Humans
MH  - *Aryl Hydrocarbon Receptor Nuclear Translocator/chemistry
MH  - *Receptors, Aryl Hydrocarbon/chemistry
MH  - Protein Multimerization
PMC - PMC10922841
MID - NIHMS1966463
COIS- Declaration of competing interest The authors declare that they have no known 
      competing financial interests or personal relationships that could have appeared 
      to influence the work reported in this paper.
EDAT- 2023/12/19 00:41
MHDA- 2024/02/19 06:43
PMCR- 2024/03/08
CRDT- 2023/12/18 19:24
PHST- 2023/08/09 00:00 [received]
PHST- 2023/12/11 00:00 [revised]
PHST- 2023/12/13 00:00 [accepted]
PHST- 2024/02/19 06:43 [medline]
PHST- 2023/12/19 00:41 [pubmed]
PHST- 2023/12/18 19:24 [entrez]
PHST- 2024/03/08 00:00 [pmc-release]
AID - S0022-2836(23)00523-5 [pii]
AID - 10.1016/j.jmb.2023.168406 [doi]
PST - ppublish
SO  - J Mol Biol. 2024 Feb 1;436(3):168406. doi: 10.1016/j.jmb.2023.168406. Epub 2023 
      Dec 16.