Journal article
ERp29 restricts connexin43 oligomerization in the endoplasmic reticulum
S Das, TD Smith, J Das Sarma, JD Ritzenthaler, J Maza, BE Kaplan, LA Cunningham, L Suaud, MJ Hubbard, RC Rubenstein, M Koval
Molecular Biology of the Cell | AMER SOC CELL BIOLOGY | Published : 2009
Abstract
Connexin43 (Cx43) is a gap junction protein that forms multimeric channels that enable intercellular communication through the direct transfer of signals and metabolites. Although most multimeric protein complexes form in the endoplasmic reticulum (ER), Cx43 seems to exit from the ER as monomers and subsequently oligomerizes in the Golgi complex. This suggests that one or more protein chaperones inhibit premature Cx43 oligomerization in the ER. Here, we provide evidence that an ER-localized, 29-kDa thioredoxin-family protein (ERp29) regulates Cx43 trafficking and function. Interfering with ERp29 function destabilized monomeric Cx43 oligomerization in the ER, caused increased Cx43 accumulatio..
View full abstractGrants
Awarded by National Institute of Diabetes and Digestive and Kidney Diseases
Funding Acknowledgements
This work was supported by National Institutes of Health grants GM-61012, HL-083120, AA-013757 (to M. K.), DK-58046 (to R.C.R.), and AA-013528 (to L. A. C.); the University Research Committee of Emory University (to M. K.); and the American Heart Association (to L. S.). R. C. R. was an Established Investigator of the American Heart Association. M. H. was supported by a Professorial Fellowship from the Melbourne Research Unit for Facial Disorders.