| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| Immediately after synthesis , very little Tg associated with calnexin ( a membrane bound molecular chaperone in the ER ) , while a larger fraction bound BiP ( a lumenal ER chaperone ) ; dissociation from these chaperones showed superficially similar kinetics . ^^^ For cells lysed either way , after in vivo reduction , Tg coprecipitated with calnexin . ^^^ After washout of dithiothreitol , nascent Tg aggregates dissolved intracellularly and were secreted ultimately . 1 h after washout , > or = 92 % of labeled Tg was found to dissociate from calnexin , while the fraction of labeled Tg bound to BiP rose from 0 to approximately 40 % , demonstrating a `` precursor product ' ' relationship . ^^^ Whereas intralumenal reduction was essential for efficient Tg coprecipitation with calnexin , Tg glycosylation was not required . ^^^ |
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| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| During its initial folding in the endoplasmic reticulum ( ER ) , newly synthesized thyroglobulin ( Tg ) is known to interact with calnexin and other ER molecular chaperones , but its interaction with calreticulin has not been examined previously . ^^^ We find that , in FRTL 5 and PC Cl 3 cells , calnexin and calreticulin interact with newly synthesized Tg in a carbohydrate dependent manner , with largely overlapping kinetics that are concomitant with the maturation of Tg intrachain disulphide bonds , preceding Tg dimerization and exit from the ER . ^^^ Calreticulin co precipitates more newly synthesized Tg than does calnexin ; however , using two different experimental approaches , calnexin and calreticulin were found in ternary complexes with Tg , making this the first endogenous protein reported in ternary complexes with calnexin and calreticulin in the ER of live cells . ^^^ Interestingly , thapsigargin treatment induces the premature exit of Tg from the calnexin / calreticulin cycle , while stabilizing and prolonging interactions of Tg with BiP ( immunoglobulin heavy chain binding protein ) and GRP 94 ( glucose regulated protein 94 ) , two chaperones whose binding is not carbohydrate dependent . ^^^ Our results suggest that calnexin and calreticulin , acting in ternary complexes with a large glycoprotein substrate such as Tg , might be engaged in the folding of distinct domains , and indicate that lumenal Ca ( 2+ ) strongly influences the folding of exportable glycoproteins , in part by regulating the balance of substrate binding to different molecular chaperone systems within the ER . . ^^^ |
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| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| This distribution overlaps that of several Golgi and vesicle markers , including mannosidase 2 , p 58 , trans Golgi network ( TGN ) 38 , and beta COP and is distinct from the endoplasmic reticulum markers calnexin and Bip . ^^^ |
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| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P27824 |
Pubmed |
SVM Score :0.0 |
| NA |
|