Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby canine kidney cells.

Breitfeld, Philip P.; Harris, Jeanne M.; Mostov, Keith E.

doi:10.1083/jcb.109.2.475

Cited by 104 publications

(101 citation statements)

References 27 publications

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“…The postendocytotic fate of a preinternalized cohort of 125 I-IgA (at 5-10 g/ml) was analyzed as described (40). In brief, filtergrown MDCK cells expressing the wild-type pIgR were treated with or without drug, and 125 I-IgA internalized from the basolateral cell surface of the cells for 10 min at 37°C.…”

Section: Methodsmentioning

confidence: 99%

“…Endocytosis of 125 I-IgA was measured as described (40). At the conclusion of the experiment, 125 I-IgA was stripped from the cell surface by incubating the cells for 60 min at 4°C with 750 mM glycine, pH 2.5, diluted 1:5 with PBS ϩ (Dulbecco's phosphate-buffered saline with 0.5 mM MgCl 2 and 0.9 mM CaCl 2 ).…”

Section: Methodsmentioning

confidence: 99%

“…Analysis of 125 I-Tf Recycling-Iron-saturated Tf was iodinated to a specific activity of 5.0 -9.0 ϫ 10 6 cpm/ g using ICl as described (40). The cells were depleted of endogenous Tf by incubating for 60 min in MEM/BSA.…”

Section: Methodsmentioning

confidence: 99%

“…There was a relatively small increase in degradation of 125 I-Tf in cytoD-treated cells (6.8% in cytoDtreated cells versus 3.7% in control cells). Since there is no known endogenous marker of the apical recycling pathway, we have measured the apical recycling of IgA internalized from the apical pole of the cells as described previously (31,40). A small fraction of the pIgR escapes cleavage at the apical cell surface and is capable of binding and endocytosing ligand (40).…”

Section: Table I Effect Of Drug Treatments On Trans-epithelial Resistmentioning

confidence: 99%

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Both Microtubules and Actin Filaments Are Required for Efficient Postendocytotic Traffic of the Polymeric Immunoglobulin Receptor in Polarized Madin-Darby Canine Kidney Cells

Maples

Ruiz

Apodaca

1997

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Table I Effect Of Drug Treatments On Trans-epithelial Resistmentioning

confidence: 99%

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Both Microtubules and Actin Filaments Are Required for Efficient Postendocytotic Traffic of the Polymeric Immunoglobulin Receptor in Polarized Madin-Darby Canine Kidney Cells

Maples

Ruiz

Apodaca

1997

Journal of Biological Chemistry

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“…With the notable exceptions of NgCAM, and polyimmunoglobulin receptor, apical proteins are likewise delivered to the apical plasma membrane without first being delivered to the basolateral surface (Breitfeld et al, 1989, Anderson et al, 2005Hua et al, 2006;Paladino et al, 2006). Delivery to apical and basolateral domains is via separate transport vesicles Sztul et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Rab8 Regulates Basolateral Secretory, But Not Recycling, Traffic at the Recycling Endosome

Henry

Sheff

2008

MBoC

108

116

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Rab8 is a monomeric GTPase that regulates the delivery of newly synthesized proteins to the basolateral surface in polarized epithelial cells. Recent publications have demonstrated that basolateral proteins interacting with the 1-B clathrin adapter subunit pass through the recycling endosome (RE) en route from the TGN to the plasma membrane. Because Rab8 interacts with these basolateral proteins, these findings raise the question of whether Rab8 acts before, at, or after the RE. We find that Rab8 overexpression during the formation of polarity in MDCK cells, disrupts polarization of the cell, explaining how Rab8 mutants can disrupt basolateral endocytic and secretory traffic. However, once cells are polarized, Rab8 mutants cause mis-sorting of newly synthesized basolateral proteins such as VSV-G to the apical surface, but do not cause mis-sorting of membrane proteins already at the cell surface or in the endocytic recycling pathway. Enzymatic ablation of the RE also prevents traffic from the TGN from reaching the RE and similarly results in mis-sorting of newly synthesized VSV-G. We conclude that Rab8 regulates biosynthetic traffic through REs to the plasma membrane, but not trafficking of endocytic cargo through the RE. The data are consistent with a model in which Rab8 functions in regulating the delivery of TGN-derived cargo to REs. INTRODUCTIONThe Rab proteins are small monomeric GTPases of the Ras family. More than 60 known Rabs collectively regulate the flow of nearly all membrane traffic within the cell (Pfeffer, 1994;Gurkan et al., 2005;Jordens et al., 2005). Of these, mammalian Rab8 has been associated with the flow of newly synthesized proteins to the basolateral surface in polarized epithelial cells (Huber et al., 1993b;Moritz et al., 2001). In yeast, the Rab8 homolog, sec4, is also required for the targeting of membrane traffic to the plasma membrane (Guo et al., 1999). It has been suggested that Rab8 may be active in delivery of secretory cargo from the TGN to the plasma membrane. (Chen et al., 1993;Huber et al., 1993b). Studies of vesicular stomatitis virus protein G (VSV-G) delivery from the trans-Golgi network (TGN) have suggested that this process is regulated by Rab8, as dominant-negative (DN) mutants of Rab8 interfere with the delivery of basolateral cargo (Huber et al., 1993b). Rab8 is not localized to the TGN; rather it is localized at or near the recycling endosome (RE) in both polarized and nonpolarized cells (Hattula et al., 2006; Roland et al., 2007). The function of Rab8 at the RE is likely to regulate recycling of membrane traffic, although its role in polarized sorting is not clear. Rab8 is not required for the delivery of all basolateral proteins, but appears to be obligatory in the case of those that bear a tyrosine-dependent basolateral-sorting determinant capable of interacting with the clathrin adapter 1-B (Ang et al., 2003). The basolateral TGN-to-plasma membrane trafficking pathway is not as direct as once thought. Recent reports demonstrate clearly that 1-B-dependent basolater...

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Disulfide bond formation between dimeric immunoglobulin A and the polymeric immunoglobulin receptor during hepatic transcytosis

et al. 1994

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The polymeric immunoglobulin receptor on rat hepatocytes binds dimeric IgA on the sinusoidal surface and mediates its transport to the canaliculus, where the complex of dimeric IgA and secretory component, the cleaved extracellular domain of polymeric immunoglobulin receptor, is secreted into bile. This process is unique in that disulfide bonds are formed between dimeric IgA and polymeric immunoglobulin receptor during transcytosis, permanently preventing their dissociation. Here we present three lines of evidence that disulfide bonding between dimeric IgA and polymeric immunoglobulin receptor occurs predominantly in a late transcytotic compartment and that hepatic transcytosis can proceed in the absence of disulfide bond formation. First, throughout the course of transcytosis the percentage of intracellular dimeric IgA disulfide bonded to polymeric immunoglobulin receptor is less than half that in bile, suggesting that disulfide bond formation is a late event in transcytosis. Second, dimeric IgA that recycles from early endocytotic compartments into the circulation is mostly noncovalently bound to secretory component. Finally, the rate of transcytosis of dimeric IgA and its appearance in bile are not affected when disulfide bond formation with polymeric immunoglobulin receptor is inhibited by blocking of free thiol groups on dimeric IgA with iodoacetamide. These results are consistent with other findings in the literature and indicate that the main physiological role of disulfide bond formation between dimeric IgA and polymeric immunoglobulin receptor is not to facilitate transcytosis but, rather, to stabilize the dimeric IgA-secretory component complex after its release into external secretions such as bile and intestinal secretions.

show abstract

Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby canine kidney cells.

Cited by 104 publications

References 27 publications

Both Microtubules and Actin Filaments Are Required for Efficient Postendocytotic Traffic of the Polymeric Immunoglobulin Receptor in Polarized Madin-Darby Canine Kidney Cells

Both Microtubules and Actin Filaments Are Required for Efficient Postendocytotic Traffic of the Polymeric Immunoglobulin Receptor in Polarized Madin-Darby Canine Kidney Cells

Rab8 Regulates Basolateral Secretory, But Not Recycling, Traffic at the Recycling Endosome

Disulfide bond formation between dimeric immunoglobulin A and the polymeric immunoglobulin receptor during hepatic transcytosis

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