The Neural Cell Adhesion Molecule Expresses a Tyrosine-independent Basolateral Sorting Signal

Gall, Annick H. Le; Powell, Stephen Joseph; Yeaman, Charles; Rodríguez-Boulan, Enrique

doi:10.1074/jbc.272.7.4559

Cited by 65 publications

(72 citation statements)

References 63 publications

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“…It has been reported that the Nglycans on the extracellular domain (26,27) or amino acid sequences within the transmembrane domain (28) of integral proteins represent important determinants for sorting to the apical membrane domain of MDCK cells. Indeed, it has been shown that deletion of the cytoplasmic tail of neural cell adhesion molecule, a basolateral protein that also belongs to the Ig superfamily, resulted in a truncated soluble form that is exclusively secreted apically (29). Further experiments will be required to determine whether some or all of the five N-glycosylation sites and/or the transmembrane domain of the Lu(v13) gp could play a role in its apical sorting.…”

Section: Discussionmentioning

confidence: 99%

Isoforms of the Lutheran/Basal Cell Adhesion Molecule Glycoprotein Are Differentially Delivered in Polarized Epithelial Cells

Nemer¹,

Colin²,

Bauvy³

et al. 1999

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Isoforms of the Lutheran/Basal Cell Adhesion Molecule Glycoprotein Are Differentially Delivered in Polarized Epithelial Cells

Nemer¹,

Colin²,

Bauvy³

et al. 1999

Journal of Biological Chemistry

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“…Basolateral targeting signals have been described for a viral protein (vesicular stomatitis virus glycoprotein G) (27); for cell adhesion molecules (NCAM and CD44) (44,45); for receptors involved in the transport of ligands (transferrin (46), polymeric immunoglobulin (15), FcIgG (47), low density lipoprotein (26), and asialoglycoprotein (25)); and for a growth factor receptor (epidermal growth factor receptor (48)). All of these signals are located in the vicinity of the membrane.…”

Section: The Basolateral Localization Signal Of the Fshr Is Differentmentioning

confidence: 99%

The Basolateral Localization Signal of the Follicle-stimulating Hormone Receptor

Beau¹,

Groyer-Picard²,

Bivic³

et al. 1998

Journal of Biological Chemistry

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The follicle-stimulating hormone receptor (FSHR) is physiologically localized in the basolateral compartment of the membrane of Sertoli cells. This localization is also observed when the receptor is experimentally expressed in Madin-Darby canine kidney cells. We thus used in vitro mutagenesis and transfection into these polarized cells to delineate the basolateral localization signal of the receptor.The signal was localized in the C-terminal tail of the intracellular domain (amino acids 678 -691) at a marked distance of the membrane. Mutation of individual amino acids highlighted the importance of Tyr 684 and Leu 689 . The 14-amino acid sequence was grafted onto the p75 neurotrophin receptor and redirected this apical protein to the basolateral cell membrane compartment. Deletion of amino acids 677-695 did not modify the internalization of the FSHR, showing that the basolateral localization signal of the FSHR is not colinear with its internalization signal.The FSH 1 receptor (FSHR), along with the LH and TSH receptors, belongs to a subgroup of G protein-coupled receptors (reviewed in Refs. 1-5). These highly homologous proteins are unusual among G protein-coupled receptors in that they contain a very large extracellular hormone binding domain. FSH transduction pathways involve mainly G s proteins coupling and the ensuing activation of adenylate cyclase (5).The FSH receptor has a central role in reproduction through the control of gonadal development and gamete production (5). In males it is expressed in testicular Sertoli cells. These cells form an epithelial blood barrier and control the development of spermatogenesis (6). In females, the FSHR is expressed in the granulosa cells of the ovaries. It controls follicular growth and, in cooperation with the LH receptor, ovarian steroidogenesis (2).Little is known of the intracellular trafficking of G proteincoupled receptors and, more specifically, of this subgroup of receptors. The pathways of internalization of the LH and TSH receptors have been studied at the ultrastructural level (7), 2 but the molecular signals involved are still unknown. The LH receptor is also present in the vascular endothelium of the testes (8). This endothelial LH receptor is involved in receptormediated hormone transcytosis, leading to the accumulation of the hormone in close proximity to the target cells. FSHR has been detected in the vascular endothelial cells of the testes (9), but its role in hormone transcytosis has not been studied to date.Another particularity of gonadotrophin and thyrostimulin receptors is their polarized cellular expression in several target tissues. Immunocytochemical studies with monoclonal antibodies have shown that the FSH receptor in Sertoli cells and the TSH receptor in thyroid follicular cells have a polarized basolateral expression (9, 10). By contrast, the LH receptor is expressed circumferentially in the ovarian granulosa and theca cells and in the testicular Leydig cells (11,12). This difference in receptor distribution could result from either a diffe...

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“…In contrast, basolateral transmembrane proteins hold discrete sorting signals exclu- sively in their cytoplasmic domains and frequently based on tyrosine (NPxY, Yxx) or dihydrophobic (LL; IL) residues. Noncanonic basolateral motifs lacking any consensus sequence have been also described (Casanova et al, 1991;Aroeti and Mostov, 1994;Le Gall et al, 1997;Odorizzi and Trowbridge, 1997;Deora et al, 2004). In addition, many basolateral proteins possess recessive apical-sorting information that becomes apparent after abrogation of their basolateral motifs (Rodriguez-Boulan et al, 2005).…”

mentioning

confidence: 99%

Polarized Traffic of LRP1 Involves AP1B and SNX17 Operating on Y-dependent Sorting Motifs in Different Pathways

Donoso

Cancino

Lee

et al. 2009

MBoC

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Low-density lipoprotein receptor-related protein 1 (LRP1) is an endocytic recycling receptor with two cytoplasmic tyrosine-based basolateral sorting signals. Here we show that during biosynthetic trafficking LRP1 uses AP1B adaptor complex to move from a post-TGN recycling endosome (RE) to the basolateral membrane. Then it recycles basolaterally from the basolateral sorting endosome (BSE) involving recognition by sorting nexin 17 (SNX17).In the biosynthetic pathway, Y 29 but not N 26 from a proximal NPXY directs LRP1 basolateral sorting from the TGN. A N 26 A mutant revealed that this NPXY motif recognized by SNX17 is required for the receptor's exit from BSE. An endocytic Y 63 ATL 66 motif also functions in basolateral recycling, in concert with an additional endocytic motif (LL 86,87 ), by preventing LRP1 entry into the transcytotic apical pathway. All this sorting information operates similarly in hippocampal neurons to mediate LRP1 somatodendritic distribution regardless of the absence of AP1B in neurons. LRP1 basolateral distribution results then from spatially and temporally segregation steps mediated by recognition of distinct tyrosine-based motifs. We also demonstrate a novel function of SNX17 in basolateral/somatodendritic recycling from a different compartment than AP1B endosomes. INTRODUCTIONEpithelial cells posses functional, morphological, and biochemically distinct apical and basolateral cell surface domains and maintain this polarized phenotype addressing specific plasma membrane proteins into each domain (Yeaman et al., 1999;Mostov, 2003;Rodriguez-Boulan et al., 2005). Apical and basolateral proteins are sorted in the biosynthetic route at the level of the trans-Golgi network (TGN; Rindler et al., 1984;Fuller et al., 1985;Griffiths and Simons, 1986), and those proteins that undergo endocytosis can be additionally sorted in recycling endosomes (RE;Mostov and Cardone, 1995;Odorizzi and Trowbridge, 1997). Evidence accumulated over a decade and consolidated in the most recent studies (Ang et al., 2004;Lock and Stow, 2005;Cancino et al., 2007;Cresawn et al., 2007;Gravotta et al., 2007) have shown that the biosynthetic route of at least some proteins includes a post-TGN transit through RE. Under this scenery, it is now important to define the relative contribution of the TGN and RE in the polarized sorting mechanisms of different cargo and in different kind of polarized cells. Neurons, for instance, have to direct distinct proteins to somato-dendritic or axonal plasma membrane domains (Rodriguez-Boulan and Powell, 1992;Winckler and Mellman, 1999), yet their protein-sorting mechanisms remain less known than in epithelial cells. A comparative analysis in epithelial cells and neurons could indeed help to understand the underlying mechanisms of the polarized phenotype.Studies in MDCK cells, the most currently used model of cell polarity, settled the basics of apical and basolateral protein sorting (Rodriguez-Boulan et al., 2005). Apical membrane proteins possess sorting information located in their extracel...

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The Neural Cell Adhesion Molecule Expresses a Tyrosine-independent Basolateral Sorting Signal

Cited by 65 publications

References 63 publications

Isoforms of the Lutheran/Basal Cell Adhesion Molecule Glycoprotein Are Differentially Delivered in Polarized Epithelial Cells

Isoforms of the Lutheran/Basal Cell Adhesion Molecule Glycoprotein Are Differentially Delivered in Polarized Epithelial Cells

The Basolateral Localization Signal of the Follicle-stimulating Hormone Receptor

Polarized Traffic of LRP1 Involves AP1B and SNX17 Operating on Y-dependent Sorting Motifs in Different Pathways

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