Identification and characterization of endoplasmic reticulum-associated protein, ERp43

miR-490-3p Modulates Cell Growth and Epithelial to Mesenchymal Transition of Hepatocellular Carcinoma Cells by Targeting Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3 (ERGIC3)

“…A previous study (48) indicated that ERp43 (ERGIC3) promoted HEK-293 cell growth. Consistently, our data demonstrated that ERGIC3 not only enhanced HCC cell viability and colony formation abilities but also stimulated cell migration and invasion ability.…”

“…Recent studies have shown that several RNA-binding proteins, such as KSRP (KHtype splicing regulatory protein) and TRBP (TAR RNA-binding protein), can interact with Drosha and Dicer complex, leading FIGURE 5. miR-490-3p promotes the cell viability, colony formation, and migration and invasion abilities in LO2 cells. A, the cell viability was measured in LO2 cells at 48,72, and 96 h after transfection by the WST-1 assay. B, colony formation ability was measured when the colony involved more than 50 cells, and then the colonies were stained by crystal violet at ϳ8 days after transfection.…”

Computational identification of root hair-specific genes in Arabidopsis

“…Two genes encode putative signaling proteins-a protein phosphatase (At4g31860) and a presumed ethylene signaling protein (At1g09740). Several loci may participate in membrane trafficking: At3g22290 encodes an evolutionarily conserved protein whose mammalian homolog, ERGIC3, is involved in ER to Golgi transport, 14 and At3g07680 codes for a member of the emp24/gp25L/p24 (IPR000348) family of membrane proteins associated with COPI and COPII vesicles, probably involved at the same transport step. 15 The product of At5g13500 was predicted to localize into the endomembrane system or organelles by the SUBA method, 16 and At5g20660 locus encodes a putative 24 kDa vacuolar protein.…”

ERGIC3 (ERGIC and golgi 3)

“…In human tumor tissues, ERGIC3 is highly expressed in lung cancer, hepatocellular carcinoma, pancreatic carcinoma, gastric carcinoma, colon cancer, esophagus cancer, but is negative in osteosarcoma, chondrosarcoma, and fibrosarcoma by immunohistochemical (IHC) staining (Lin, 2014). In addtion, ERGIC3 is highly expressed in the spinal cord and kidney of mouse (Nishikawa et al, 2007).…”

“…There is a strong interaction between ERGIC3 and ERGIC2 so as to form a heteromer complex which exerting its biological function. The complex may be involved in : 1) the sorting of some secretory molecules during vesiclar transport (Belden and Barlowe, 2001;Otte and Barlowe, 2004) due to the hydrophobic signals present on both C-terminal tails of the ERGIC3-ERGIC2 complex control sorting into COPII vesicles for anterograde transport, and retrieval from the Golgi is mediated by a COPI binding KKxx motif on ERGIC3 (Otte and Barlowe, 2002) ; 2) protein folding and glycoprotein processing in the endoplasmic reticulum and cis-Golgi network (Nishikawa et al, 2007;Welsh et al, 2006). Glucosidase II is not transported into COPII vesicles in vitro as well as cells lacking a cycling ERGIC3-ERGIC2 complex have a mild glycoprotein processing defect and a partial loss of glucosidase (Leah, 2006) inhibiting endoplasmic reticulum stress (ERS)-induced cell death by tunicamycin in HEK-293 cells (Nishikawa et al, 2007).…”