Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P11021 (BiP)
 2,049 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mouse Wnt-1 gene, a target for insertional activation in mouse mammary tumor virus-induced mammary tumors, encodes poorly secreted, cysteine-rich glycoproteins required for proper central nervous system development. We have been analyzing the biosynthesis of Wnt-1 proteins in several cell lines that express Wnt-1 cDNA from heterologous promoters. A protein of 78 kDa was found to be associated with the intracellular forms of Wnt-1 proteins in mammalian and avian cells by using multiple antisera against Wnt-1 proteins. We have identified p78 as the binding protein BiP with anti-BiP antisera and by its release from Wnt-1 immunoprecipitates upon incubation with MgCl2 and ATP. Experiments with a Wnt-1 mutant that lacks the sequence encoding the signal peptide indicates that Wnt-1 proteins must enter the secretory pathway in order to interact with BiP. We demonstrate that Wnt-1 proteins are associated with BiP in cells in which active Wnt-1 proteins are produced, such as a cultured mammary epithelial cell line and Wnt-1 transgenic mouse mammary tumor cells. The association of Wnt-1 proteins with BiP may be a factor in determining the efficiency of secretion of Wnt-1 gene products.
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PMID:Interaction of Wnt-1 proteins with the binding protein BiP. 153 Oct 88

To analyze the early events occurring during the folding and assembly of major histocompatibility complex class I antigens, we used a panel of P815 mouse mastocytoma transfectants expressing wild-type or mutant human leukocyte antigen (HLA)-Cw3 proteins. We observed that newly synthesized unassembled HLA-Cw3 heavy chains (Cw3 alpha) specifically associate with three major long-lived proteins denoted p105, p88 and p78, according to their size. These proteins display different kinetics of interaction. The association of p105 is transient, while p78, which we identified as the immunoglobulin binding protein BiP, interacts permanently with Cw3 alpha chains. Furthermore, the binding of p88, a calnexin candidate, seems delayed compared to that of p105 and p78. As the great majority of newly synthesized Cw3 alpha proteins expressed in P815 cells can associate with cotransfected human beta 2-microglobulin (beta 2m), our observations suggest that multiple molecular chaperones cooperate in the folding of class I heavy chains. We were unable to coimmunoprecipitate detectable levels of these proteins with oligomerized Cw3 alpha chains. However, we could still detect p78/BiP in transient association with mutant HLA-Cw3 heterodimers which were delayed in the endoplasmic reticulum (ER) compared to their wild-type counterparts. In this case, the dissociation of BiP preceded the ER to Golgi transport of these proteins. These results suggest that BiP release is neither related to the process of class I oligomerization nor to the ER retention of class I assembly intermediates.
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PMID:Biogenesis of MHC class I antigens: involvement of multiple chaperone molecules. 795 6

The folding and trafficking of tropoelastin is thought to be mediated by intracellular chaperones, although the identity and role of any tropoelastin chaperone remain to be determined. To identify proteins that are associated with tropoelastin intracellularly, bifunctional chemical cross-linkers were used to covalently stabilize interactions between tropoelastin and associated proteins in the secretory pathway in intact fetal bovine auricular chondrocytes. Immunoprecipitation of tropoelastin from cell lysates after cross-linking and analysis by SDS-PAGE showed the presence of two proteins of approximately 74 kD (p74) and 78 kD (p78) that coimmunoprecipitated with tropoelastin. Microsequencing of peptide fragments from a cyanogen bromide digest of p78 identified this protein as BiP and sequence analysis identified p74 as the peptidyl-prolyl cis-trans isomerase, FKPB65. The appearance of BiP and FKBP65 in the immunoprecipitations could be enhanced by the addition of brefeldin A (BFA) and N-acetyl-leu-leu-norleucinal (ALLN) to the culture medium for the final 4 h of labeling. Tropoelastin accumulates in the fused ER/Golgi compartment in the presence of BFA if its degradation is inhibited by ALLN (Davis, E.C., and R.P. Mecham. 1996. J. Biol. Chem. 271:3787-3794). The use of BFA and other secretion-disrupting agents suggests that the association of tropoelastin with FKBP65 occurs in the ER. Results from this study provide the first identification of a ligand for an FKBP in the secretory pathway and suggest that the prolyl cis-trans isomerase activity of FKBP65 may be important for the proper folding of the proline-rich tropoelastin molecule before secretion.
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PMID:Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway. 944 5