What is GRP78 gene?
GRP78 (HSPA5), also referred to as ‘immunoglobulin heavy chain-binding protein’ (BiP), is a member of the heat-shock protein-70 (HSP70) family and involved in the folding and assembly of proteins in the ER. The level of BiP is strongly correlated with the amount of secretory proteins (e.g. IgG) within the ER.
Where is GRP78 located?
GRP78 is located mainly in the ER, but it has also been observed in the cytoplasm, the mitochondria, the nucleus, the plasma membrane, and secreted, although it is dedicated mostly to engage endogenous cytoprotective processes.
What type of chaperone is HSP70?
Abstract. Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins.
Is SEC 61 a Translocon?
Sec61, termed SecYEG in prokaryotes, is a membrane protein complex found in all domains of life. As the core component of the translocon, it transports proteins to the endoplasmic reticulum in eukaryotes and out of the cell in prokaryotes.
What is the difference between Hsp70 and Hsc70?
For example, the heat shock cognate 70 (Hsc70) group is defined by its constitutive expression and cytoplasmic localization. The Hsp70 group on the other hand is induced by cellular stress such as temperature changes or exposure to toxic chemicals.
What is the difference between Hsp60 and Hsp70?
Hsp70 is a simple chaperone that is found in all living organisms. It functions to protect unfolded proteins. Hsp60 is a molecular machine that functions to isolate unfolded proteins and provide the optimal environment for on-pathway folding. Hsp70 is a single, monomeric protein that is found throughout the cell.
What does the translocon do?
In eukaryotes the term translocon most commonly refers to the complex that transports nascent polypeptides with a targeting signal sequence into the interior (cisternal or lumenal) space of the endoplasmic reticulum (ER) from the cytosol.
Is Calnexin a transmembrane?
Calnexin is a transmembrane protein and calreticulin is the soluble luminal homolog. Both proteins interact with monoglucosylated, trimmed intermediates of N-linked core glycans on nascent glycoproteins.
What is the function of CHOP?
CHOP belongs to the family of CCAAT/enhancer binding proteins (C/EBPs) and is involved in the regulation of genes that encode proteins involved in proliferation, differentiation and expression, and energy metabolism. CHOP is a 29 kD protein with 169 (human) or 168 (rodents) amino acid residues.