Document Detail

TRAM1 is involved in disposal of ER membrane degradation substrates.
MedLine Citation:
PMID:  20430023     Owner:  NLM     Status:  MEDLINE    
ER quality control consists of monitoring protein folding and targeting misfolded proteins for proteasomal degradation. ER stress results in an unfolded protein response (UPR) that selectively upregulates proteins involved in protein degradation, ER expansion, and protein folding. Given the efficiency in which misfolded proteins are degraded, there likely exist cellular factors that enhance the export of proteins across the ER membrane. We have reported that translocating chain-associated membrane protein 1 (TRAM1), an ER-resident membrane protein, participates in HCMV US2- and US11-mediated dislocation of MHC class I heavy chains (Oresic, K., Ng, C.L., and Tortorella, D. 2009). Consistent with the hypothesis that TRAM1 is involved in the disposal of misfolded ER proteins, cells lacking TRAM1 experienced a heightened UPR upon acute ER stress, as evidenced by increased activation of unfolded protein response elements (UPRE) and elevated levels of NF-kappaB activity. We have also extended the involvement of TRAM1 in the selective degradation of misfolded ER membrane proteins Cln6(M241T) and US2, but not the soluble degradation substrate alpha(1)-antitrypsin null(HK). These degradation model systems support the paradigm that TRAM1 is a selective factor that can enhance the dislocation of ER membrane proteins.
Caroline L Ng; Kristina Oresic; Domenico Tortorella
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-04-27
Journal Detail:
Title:  Experimental cell research     Volume:  316     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-08     Completed Date:  2010-07-29     Revised Date:  2013-05-10    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2113-22     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Elsevier Inc. All rights reserved.
One Gustave L. Levy Place, Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029, USA.
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MeSH Terms
Blotting, Western
Cells, Cultured
Endoplasmic Reticulum / metabolism*
Intracellular Membranes / metabolism*
Kidney / cytology,  metabolism
Luciferases / metabolism
Membrane Glycoproteins / physiology*
Membrane Proteins / metabolism*
Membrane Transport Proteins / physiology*
NF-kappa B / genetics,  metabolism
Protein Transport
RNA, Messenger / genetics
Reverse Transcriptase Polymerase Chain Reaction
Unfolded Protein Response / physiology
alpha 1-Antitrypsin / metabolism*
Grant Support
Reg. No./Substance:
0/CLN6 protein, human; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Membrane Transport Proteins; 0/NF-kappa B; 0/RNA, Messenger; 0/TRAM1 protein, human; 0/alpha 1-Antitrypsin; EC 1.13.12.-/Luciferases

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