Apical secretion of hepatitis B surface antigen from transfected Madin-Darby canine kidney cells.

González, Alfonso; Nicovani, Sandra; F, Juica

doi:10.1016/s0021-9258(18)53301-9

Cited by 22 publications

(5 citation statements)

References 66 publications

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“…These results confirm and extend conclusions that we and others presented previously, that N-glycans are not necessary for apical sorting of influenza virus hemagglutinin (Roth et al, 1979;Green et al, 1981). Our findings are also consistent with reports that apical sorting of several other proteins is independent of N-glycosylation (Lisanti et al, 1989(Lisanti et al, , 1990Ullrich et al, 1991;Ragno et al, 1992;Gonzalez et al, 1993), and that many N-glycosylated proteins are poorly sorted in MDCK cells (Stephens and Compans, 1986;Soole et al, 1992;Geffen et al, 1993;Haller and Alper, 1993;Thomas et al, 1993;Le Gall et al, 1997). However, these data are not inconsistent with the possible involvement of N-glycans in sorting of a subset of apical proteins (Urban et al, 1987;Kitigawa et al, 1994;Scheiffele et al, 1995).…”

Section: N-glycans Are Not Necessary For Apical Sorting Of Membrane-anchored or Soluble Forms Of P75 Ntrsupporting

confidence: 94%

The O-glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells

Yeaman

Gall²,

Baldwin³

et al. 1997

The Journal of Cell Biology

271

242

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Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75NTR causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75NTR does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75NTR is not required for apical sorting of either transmembrane or secreted forms.

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Section: N-glycans Are Not Necessary For Apical Sorting Of Membrane-anchored or Soluble Forms Of P75 Ntrsupporting

confidence: 94%

The O-glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells

Yeaman

Gall²,

Baldwin³

et al. 1997

The Journal of Cell Biology

271

242

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“…Glycolipid anchors direct proteins to the apical surface of several types of epithelial cells (Brown et al, 1989;Lisanti et al, 1989), apparently by associating in the trans -Golgi network (TGN) with detergent-insoluble membrane domains enriched in glycosphingolipids and cholesterol (Simons and Ikonen, 1997). Oligosaccharides on some secreted proteins appear to specify apical transport (Scheiffele et al, 1997), although this mechanism does not apply to all secreted proteins (Ullrich et al, 1991;Ragno et al, 1992;Soole et al, 1992;Gonzalez et al, 1993;Yeaman et al, 1997) and has not been conclusively demonstrated for membrane bound proteins (Green et al, 1981;Geffen et al, 1993;Haller and Alper, 1993;Thomas et al, 1993;Stephens and Compans, 1986;Le Gall et al, 1997). The transmembrane segments of the influenza virus neuraminidase and the simian virus 5 hemagglutinin neuraminidase specify apical transport (Kundu et al, 1996;Huang et al, 1997).…”

mentioning

confidence: 99%

Mutations in the Middle of the Transmembrane Domain Reverse the Polarity of Transport of the Influenza Virus Hemagglutinin in MDCK Epithelial Cells

Lin

Naim

Rodríguez

et al. 1998

The Journal of Cell Biology

189

220

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The composition of the plasma membrane domains of epithelial cells is maintained by biosynthetic pathways that can sort both proteins and lipids into transport vesicles destined for either the apical or basolateral surface. In MDCK cells, the influenza virus hemagglutinin is sorted in the trans-Golgi network into detergent-insoluble, glycosphingolipid-enriched membrane domains that are proposed to be necessary for sorting hemagglutinin to the apical cell surface. Site- directed mutagenesis of the hemagglutinin transmembrane domain was used to test this proposal. The region of the transmembrane domain required for apical transport included the residues most conserved among hemagglutinin subtypes. Several mutants were found to enter detergent-insoluble membranes but were not properly sorted. Replacement of transmembrane residues 520 and 521 with alanines converted the 2A520 mutant hemagglutinin into a basolateral protein. Depleting cell cholesterol reduced the ability of wild-type hemagglutinin to partition into detergent-insoluble membranes but had no effect on apical or basolateral sorting. In contrast, cholesterol depletion allowed random transport of the 2A520 mutant. The mutant appeared to lack sorting information but was prevented from reaching the apical surface when detergent-insoluble membranes were present. Apical sorting of hemagglutinin may require binding of either protein or lipids at the middle of the transmembrane domain and this normally occurs in detergent-insoluble membrane domains. Entry into these domains appears necessary, but not sufficient, for apical sorting.

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“…The eluted proteins were diluted to 1 ml with RIPA and subjected to NeutrAvidin–Agarose precipitation to isolate surface-located Shh. Secreted Shh was immunoprecipitated from the apical and basolateral media with protein-A–Sepharose-bound 5E1, as described for other proteins ( Gonzalez et al, 1987 ; Gonzalez et al, 1993 ; Marzolo et al, 1997 ). The immune complexes of surface-located and secreted Shh were resolved by SDS-PAGE, and [ 35 S]-methionine/cysteine-labeled proteins were developed in the Cyclone Plus scanner (PerkinElmer) using OptiQuant software (3.0, PerkinElmer).…”

Section: Methodsmentioning

confidence: 99%

Sonic hedgehog is basolaterally sorted from the TGN and transcytosed to the apical domain involving Dispatched-1 at Rab11-ARE

Sandoval

Labarca

Retamal

et al. 2022

Front. Cell Dev. Biol.

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Hedgehog proteins (Hhs) secretion from apical and/or basolateral domains occurs in different epithelial cells impacting development and tissue homeostasis. Palmitoylation and cholesteroylation attach Hhs to membranes, and Dispatched-1 (Disp-1) promotes their release. How these lipidated proteins are handled by the complex secretory and endocytic pathways of polarized epithelial cells remains unknown. We show that polarized Madin–Darby canine kidney cells address newly synthesized sonic hedgehog (Shh) from the TGN to the basolateral cell surface and then to the apical domain through a transcytosis pathway that includes Rab11-apical recycling endosomes (Rab11-ARE). Both palmitoylation and cholesteroylation contribute to this sorting behavior, otherwise Shh lacking these lipid modifications is secreted unpolarized. Disp-1 mediates first basolateral secretion from the TGN and then transcytosis from Rab11-ARE. At the steady state, Shh predominates apically and can be basolaterally transcytosed. This Shh trafficking provides several steps for regulation and variation in different epithelia, subordinating the apical to the basolateral secretion.

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Apical secretion of hepatitis B surface antigen from transfected Madin-Darby canine kidney cells.

Cited by 22 publications

References 66 publications

The O-glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells

The O-glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells

Mutations in the Middle of the Transmembrane Domain Reverse the Polarity of Transport of the Influenza Virus Hemagglutinin in MDCK Epithelial Cells

Sonic hedgehog is basolaterally sorted from the TGN and transcytosed to the apical domain involving Dispatched-1 at Rab11-ARE

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