Author:
Turano Carlo,Gaucci Elisa,Grillo Caterina,Chichiarelli Silvia
Abstract
AbstractThe protein ERp57/GRP58 is a stress-responsive protein and a component of the protein disulfide isomerase family. Its functions in the endoplasmic reticulum are well known, concerning mainly the proper folding and quality control of glycoproteins, and participation in the assembly of the major histocompatibility complex class 1. However, ERp57 is present in many other subcellular locations, where it is involved in a variety of functions, primarily suggested by its participation in complexes with other proteins and even with DNA. While in some instances these roles need to be confirmed by further studies, a great number of observations support the participation of ERp57 in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair.
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference88 articles.
1. Nuclear localization and DNA interaction of protein disulfide isomerase ERp in mammalian cells http dx org;Coppari;Cell Biochem,2002
2. A stress - regulated protein a member of thioredoxin superfamily , is a carnitine palmitoyltransferase isoenzyme;Murthy;Biochem J,1994
3. Protein degradation by the phosphoinositide - specific phospholipase - alpha family from rat liver endoplasmic reticulum;Urade;Biol Chem,1992
4. Involvement of MARRS membrane associated , rapid response steroid - binding , a novel vitamin D receptor , in growth inhibition of breast cancer cells http dx org;Richard;Exp Cell Res,2010
5. membrane translocation dictates the immunogenicity of tumor cell death by controlling the membrane translocation of calreticulin;Obeid;Immunol,2008
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