By Paul Eggleton
The booklet makes a speciality of the newest discoveries on calreticulin, calnexin and different endoplasmic reticulum proteins. Calreticulin has been implicated to impact various mobile functionality and play a task in lots of pathologies together with protein folding problems, cardiac pathologies, melanoma and autoimmunity. This publication comprises contributions from the realm leaders within the quarter of endoplasmic reticulum functionality, protein folding, Calcium homeostasis and autoimmunity. It increases many exciting questions on calreticulin, calnexin and the endoplasmic reticulum and offers a special chance to gain the importance of those calcium-binding chaperones. The publication is exclusive in each recognize and we're not conscious of the other book concentrating on those features of endoplasmic reticulum biology. due to a crucial position of endoplasmic reticulum, calreticulin and calnexin in nearly all mobile services, the booklet could be of curiosity to every person within the organic sciences.
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Additional resources for Calreticulin (Molecular Biology Intelligence Unit)
Example text
35. Frickel EM, Riek R, Jelesarov I et al. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci USA 2002; 99:1954-9. 36. Khanna NC, Tokuda M, Waisman DM. Conformational changes induced by binding of divalent cations to calregulin [published erratum appears in J Biol Chem 1986 Dec 5; 261(34):16279]. J Biol Chem 1986; 261:8883-7. 37. Saito Y, Ihara Y, Leach MR et al. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins.
Disulphide Bridge Full-length calreticulin contains a disulphide bond in the N-terminal half of the molecule, which has been demonstrated to be important for the chaperone function of calreticulin, and hence it must play an important role in the folding of the protein and its ability to interact with specific substrates. 22,23 This is inconsistent with data published on bovine brain material14 but is in agreement with the sequence homologies with calnexin and calmegin as there is no equivalent of calreticulin’s Cys146 in these proteins.
Here we review work on calnexin/calreticulin-assisted glycoprotein folding in the ER, with an emphasis on recent molecular and structural studies. The ER As a Compartment for Protein Folding and Quality Control The majority of secretory proteins, plasma membrane proteins, and proteins of the secretory and endocytic pathways in eukariotic cells are synthesized on membrane-bound ribosomes, and undergo maturation in the endoplasmic reticulum (ER). The ER is responsible for translocation, modification, folding, oligomeric assembly, and quality control.