Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.

Bole, David G.; Hendershot, Linda M.; Kearney, John F.

doi:10.1083/jcb.102.5.1558

Cited by 888 publications

(598 citation statements)

References 47 publications

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“…The role of BiP could be to retain the misfolded proteins. The inhibition of N-glycosylation increased the association with BiP, as shown for immunoglobulin heavy chains (BOLE et al 1986) and several human serum glycoproteins (DORNER et al 1987). The extent and stability of BiP association were inversely correlated with secretion efficiency.…”

Section: Retention Of Proteins In the Ermentioning

confidence: 84%

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

Langer¹,

Neupert²

1991

Current Topics in Microbiology and Immunology

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Section: Retention Of Proteins In the Ermentioning

confidence: 84%

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

Langer¹,

Neupert²

1991

Current Topics in Microbiology and Immunology

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“…GRP78-BiP was identified independently by different groups through its increased expression in cells deprived of glucose in lymphoid cells and by its association with Ig heavy chains that are not associated with Ig light chains (Haas and Wabl, 1983;Bole et al, 1986). The polypeptides identified by these groups were later shown to be identical, thus linking its glucose-regulated expression with a biochemical property (Munro and Pelham, 1986).…”

Section: Introductionmentioning

confidence: 96%

“…As GRP78-BiP has often been found associated in a semistable manner with incompletely assembled or malfolded proteins, it has been proposed that it may play a role in retention of proteins in the ER (Bole et al, 1986;Dorner et al, 1987;. Therefore, it was of interest to investigate the fate of the HN truncation and deletion mutants in the exocytic pathways given their differing association with GRP78-BiP.…”

Section: Intracellular Localization Of Hn Mutant Proteinsmentioning

confidence: 99%

“…A rat monoclonal antibody (anti-BiP), specific for the cellular heavy chain binding protein (BiP), was kindly provided by Dr. Linda Hendershot, St. Jude Children's Research Hospital, Memphis, TN (Bole et al, 1986). A rabbit polyclonal antiserum prepared against chicken pyruvate kinase (anti-PK) that also recognizes simian PK was described previously (Hiebert and Lamb, 1988).…”

Section: Antibodiesmentioning

confidence: 99%

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Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.

Watowich

Lamb

1992

MBoC

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The endoplasmic reticulum (ER)-localized chaperone protein, GRP78-BiP, is involved in the folding and oligomerization of secreted and membrane proteins, including the simian virus 5 hemagglutinin-neuraminidase (HN) glycoprotein. To understand this interaction better, we have constructed a series of HN mutants in which specific portions of the extracytoplasmic domain have been deleted. Analysis of these mutant polypeptides expressed in CV-1 cells have indicated that GRP78-BiP binds to selective sequences in HN and that there exists more than a single site of interaction. Mutant polypeptides have been characterized that are competent and incompetent for association with GRP78-BiP. These mutants have been used to show that the induction of GRP78-BiP synthesis due to the presence of nonnative protein molecules in the ER is dependent on GRP78-BiP complex formation with its substrates. These studies have implications for the function of the GRP78-BiP protein and the mechanism by which the gene is regulated. INTRODUCTIONThe 78-kDa glucose-regulated/Ig heavy-chain binding protein (GRP78-BiP) is a member of the highly con-

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“…To distinguish between these possibilities, two experiments were performed. First, we tested whether a soluble resident of the ER lumen (BiP), a protein actively retrieved from the Golgi by the KDEL receptor pathway (Bole et al, 1986;Lewis and Pelham, 1992;Orci et al, 1997), is inappropriately secreted in hSac1-depleted cell populations. This is expected if hSac1 is required for formation of COP1 vesicles that help retrieve BiP.…”

Section: Functional Distinction Between Mammalian Sac1 and Arf Depletionmentioning

confidence: 99%

The Sac1 Phosphoinositide Phosphatase Regulates Golgi Membrane Morphology and Mitotic Spindle Organization in Mammals

Liu

Boukhelifa

Tribble

et al. 2008

MBoC

131

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Phosphoinositides (PIPs) are ubiquitous regulators of signal transduction events in eukaryotic cells. PIPs are degraded by various enzymes, including PIP phosphatases. The integral membrane Sac1 phosphatases represent a major class of such enzymes. The central role of lipid phosphatases in regulating PIP homeostasis notwithstanding, the biological functions of Sac1-phosphatases remain poorly characterized. Herein, we demonstrate that functional ablation of the single murine Sac1 results in preimplantation lethality in the mouse and that Sac1 insufficiencies result in disorganization of mammalian Golgi membranes and mitotic defects characterized by multiple mechanically active spindles. Complementation experiments demonstrate mutant mammalian Sac1 proteins individually defective in either phosphoinositide phosphatase activity, or in recycling of the enzyme from the Golgi system back to the endoplasmic reticulum, are nonfunctional proteins in vivo. The data indicate Sac1 executes an essential household function in mammals that involves organization of both Golgi membranes and mitotic spindles and that both enzymatic activity and endoplasmic reticulum localization are important Sac1 functional properties. INTRODUCTIONSpatial and temporal regulation of intracellular signaling in eukaryotic cells involves the compartmentalization of membrane surfaces into discrete, albeit often transient, functional units. There are several biochemical strategies by which cells generate such units or domains. One well-established strategy uses the chemical diversity offered by phosphoinositides (PIPs), i.e., phosphorylated forms of phosphatidylinositol (PtdIns) (Majerus, 1997;Fruman et al., 1998;Strahl and Thorner, 2007). The chemical heterogeneity of individual PIP species permits the construction of chemically unique platforms on membrane surfaces that, in turn, recruit unique cohorts of proteins that drive specific biological reactions. Spatial and temporal control of such reactions requires a finely coordinated balance between the activities of the lipid kinases that produce PIPs and the activities of enzymes that degrade them. PIP turnover is catalyzed by two general classes of enzymes: phospholipases and PIP phosphatases.Although experimental scrutiny of the phospholipases has historically been more intense, recent demonstrations of the significant biological functions played by PTEN, the myotubularins, and synaptojanins highlight the general importance of PIP phosphatases (Wishart et al., 2001;Wishart and Dixon, 2002;Wenk and De Camilli, 2004).The SAC domain derives from the yeast Sac1 protein (ySac1; Cleves et al., 1989), and it represents a signature for PIP phosphatase catalytic activity . PIP phosphatases such as phosphatase and tensin homolog (mutated in multiple advanced cancers 1) (PTEN) (Maehama et al., 2001), synaptojanins (Cremona et al., 1999), and synaptojanin-like proteins (Srinivasan et al., 1997;Stolz et al., 1998) all harbor SAC domains. The prototypical member of this family, ySac1, catalyzes the dephosphoryla...

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Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.

Cited by 888 publications

References 47 publications

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.

The Sac1 Phosphoinositide Phosphatase Regulates Golgi Membrane Morphology and Mitotic Spindle Organization in Mammals

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