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Molecular characterization of the endoplasmic reticulum: Insights from proteomic studies
Author(s) -
Chen Xuequn,
Karnovsky Alla,
Sans Maria Dolors,
Andrews Philip C.,
Williams John A.
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000234
Subject(s) - endoplasmic reticulum , proteome , endoplasmic reticulum associated protein degradation , biology , proteomics , microbiology and biotechnology , organelle , unfolded protein response , shotgun proteomics , golgi apparatus , biochemistry , gene
The endoplasmic reticulum (ER) is a multifunctional intracellular organelle responsible for the synthesis, processing and trafficking of a wide variety of proteins essential for cell growth and survival. Therefore, comprehensive characterization of the ER proteome is of great importance to the understanding of its functions and has been actively pursued in the past decade by scientists in the proteomics field. This review summarizes major proteomic studies published in the past decade that focused on the ER proteome. We evaluate the data sets obtained from two different organs, liver and pancreas each of which contains a primary cell type (hepatocyte and acinar cell) with specialized functions. We also discuss how the nature of the proteins uncovered is related to the methods of organelle purification, organelle purity and the techniques used for protein separation prior to MS. In addition, this review also puts emphasis on the biological insights gained from these studies regarding the molecular functions of the ER including protein synthesis and translocation, protein folding and quality control, ER‐associated degradation and ER stress, ER export and membrane trafficking, calcium homeostasis and detoxification and drug metabolism.