Document Detail


The psoriasis-associated D10N variant of the adaptor Act1 with impaired regulation by the molecular chaperone hsp90.
MedLine Citation:
PMID:  23202271     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Act1 is an essential adaptor in interleukin 17 (IL-17)-mediated signaling and is recruited to the receptor for IL-17 after stimulation with IL-17. Here we found that Act1 was a 'client' protein of the molecular chaperone hsp90. The D10N variant of Act1 (Act1(D10N)) that is linked to susceptibility to psoriasis was defective in its interaction with hsp90, which resulted in a global loss of Act1 function. Act1-deficient mice modeled the mechanistic link between loss of Act1 function and susceptibility to psoriasis. Although Act1 was necessary for IL-17-mediated inflammation, Act1-deficient mice had a hyperactive response of the T(H)17 subset of helper T cells and developed spontaneous IL-22-dependent skin inflammation. In the absence of IL-17 signaling, IL-22 was the main contributor to skin inflammation, which provides a molecular mechanism for the association of Act1(D10N) with psoriasis susceptibility.
Authors:
Chenhui Wang; Ling Wu; Katarzyna Bulek; Bradley N Martin; Jarod A Zepp; Zizhen Kang; Caini Liu; Tomasz Herjan; Saurav Misra; Julie A Carman; Ji Gao; Ashok Dongre; Shujie Han; Kevin D Bunting; Jennifer S Ko; Hui Xiao; Vijay K Kuchroo; Wenjun Ouyang; Xiaoxia Li
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-12-02
Journal Detail:
Title:  Nature immunology     Volume:  14     ISSN:  1529-2916     ISO Abbreviation:  Nat. Immunol.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-14     Completed Date:  2013-03-01     Revised Date:  2013-04-16    
Medline Journal Info:
Nlm Unique ID:  100941354     Medline TA:  Nat Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  72-81     Citation Subset:  IM    
Affiliation:
Department of Immunology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Connexin 43 / genetics,  immunology,  metabolism*
Disease Models, Animal
Genetic Predisposition to Disease
HSP90 Heat-Shock Proteins / metabolism*
Humans
Interleukin-17 / metabolism
Mice
Mice, Knockout
Molecular Chaperones / genetics,  metabolism*
Mutation / genetics
Peptide Fragments / genetics,  immunology,  metabolism*
Polymorphism, Genetic
Protein Binding / genetics,  immunology
Psoriasis / genetics,  immunology*
Signal Transduction
Th17 Cells / immunology*
Grant Support
ID/Acronym/Agency:
1P01 HL103453/HL/NHLBI NIH HHS; 1R01NS071996/NS/NINDS NIH HHS; P01 HL103453/HL/NHLBI NIH HHS; R01 GM080271/GM/NIGMS NIH HHS; R01 NS071996/NS/NINDS NIH HHS; T32 AI89474-1/AI/NIAID NIH HHS; T32 GM007250/GM/NIGMS NIH HHS; UL1 TR000439/TR/NCATS NIH HHS
Chemical
Reg. No./Substance:
0/ACT1 protein; 0/Connexin 43; 0/HSP90 Heat-Shock Proteins; 0/Interleukin-17; 0/Molecular Chaperones; 0/Peptide Fragments
Comments/Corrections
Comment In:
Nat Immunol. 2013 Jan;14(1):16-7   [PMID:  23238753 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Shared and distinct transcriptional programs underlie the hybrid nature of iNKT cells.
Next Document:  Conformational states of the kinase Lck regulate clustering in early T cell signaling.