Function
When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), a member of the heat-shock protein-70 (HSP70) family is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Furthermore could be observed that the level of GRP78 is strongly correlated with the amount of secretory proteins (e.g. IgG) within the ER. Because so many ER proteins interact transiently with GRP78, it is presumed that it may play a key role in monitoring protein transport through the cell.
Read more about this topic: Binding Immunoglobulin Protein
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