Sorting nexin 17 facilitates LRP recycling in the early endosome

Kerkhof, Peter van; Lee, Jiyeon; McCormick, Lynn M.; Tetrault, Elena; Lü, Wenyan; Schoenfish, Marissa J.; Oorschot, Viola; Strous, Ger J.; Klumperman, Judith; Bu, Guojun

doi:10.1038/sj.emboj.7600756

Cited by 141 publications

(179 citation statements)

References 38 publications

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“…For example, SNX17 has been reported to promote the membrane recycling of LRP (LDL Receptorrelated Protein) by preventing the sorting of this receptor to lysosomes for degradation [55]. Our data does not support a role of SLIC-1 in the regulation of PSGL-1 recycling and/or degradation.…”

Section: Discussioncontrasting

confidence: 51%

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

Schaff¹,

Shih²,

Lorenz³

et al. 2008

Eur J Immunol

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P-Selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of leukocytes that serves as the major ligand for the selectin family of adhesion molecules and functions in leukocyte tethering and rolling on activated endothelium and platelets. Previous studies have implicated the highly conserved cytoplasmic domain of PSGL-1 in regulating outside-in signaling of integrin activation. However, molecules that physically and functionally interact with this domain are not completely defined. Using a yeast two-hybrid screen with the cytoplasmic domain of PSGL-1 as bait, a novel protein designated selectin ligand interactor cytoplasmic-1 (SLIC-1) was isolated. Computer-based homology search revealed that SLIC-1 was the human orthologue for the previously identified mouse sorting nexin 20. Direct interaction between SLIC-1 and PSGL-1 was specific as indicated by co-immunoprecipitation and motif mapping. Colocalization experiments demonstrated that SLIC-1 contains a Phox homology domain that binds phosphoinositides and targets the PSGL-1/SLIC-1 complex to endosomes. Deficiency in the murine homologue of SLIC-1 did not modulate PSGL-1-dependent signaling nor alter neutrophil adhesion through PSGL-1. We conclude that SLIC-1 serves as a sorting molecule that cycles PSGL-1 into endosomes with no impact on leukocyte recruitment.Supporting Information for this article is available at http://www.wiley-vch.de/contents/jc_2040/2008/37777_s.pdf IntroductionThe initial tethering and rolling of leukocytes on activated endothelium and platelets is a key biological event mediated by P-selectin glycoprotein ligand-1 (PSGL-1), a mucin-like glycoprotein that functions as a unique high-affinity ligand for the selectin family of adhesion molecules (for reviews, see [1][2][3][4]). Structurally, PSGL-1 is a type I integral membrane protein consisting of an N-terminal selectin-binding domain followed by a region of multiple decameric repeats bearing O-linked glycans, a short transmembrane domain, and lastly a cytoplasmic tail [5][6][7][8][9][10]. Comparison of human and murine PSGL-1 reveals that the 69-amino acid intracellular domain of PSGL-1 is highly conserved. While overall identity between human and Abbreviations: EEA-1: early endosomal antigen-1 Á EGFP: enhanced green fluorescent protein Á ERM: ezrin/radixin/ moesin Á L-E/I: L cell monolayer expressing E-selectin and ICAM-1 Á PI: phosphatidylinositol Á PI 3-kinase: phosphatidylinositol 3-kinase Á PSGL-1: P-selectin glycoprotein ligand-1 Á PtdIns(3)P: phosphatidylinositol 3-phosphate Á PtdIns(3,4)P 2 : phosphatidylinositol 3,4-bisphosphate Á PtdIns(3,4,5)P 3 : phosphatidylinositol 3,4,5-trisphosphate Á PX domain: phox homology domain Á SLIC-1: selectin ligand interactor cytoplasmic-1 Á SNX20: sorting nexin 20 Á TM: transmembrane Ulrich Y. Schaff et al.

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Section: Discussioncontrasting

confidence: 51%

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

Schaff¹,

Shih²,

Lorenz³

et al. 2008

Eur J Immunol

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“…At 5 min of antibody quenching, the measured recycling efficiency of cells expressing the wild-type mLRP4 was around 27%, compared with Ͻ2% for cells expressing the N 26 A mutant. After 20 min of quenching, the efficiency of recycling for the mutant was still very low (7% compared with 26% of the control).Taken together, all these results demonstrate that recycling of the mutant N 26 A receptor is severely impaired (Figure 8B) and more dramatically than in nonpolarized cells (van Kerkhof et al, 2005). Thus the lack of surface localization of this mutant at the steady state is most likely due to abrogation of a motif that promotes recycling.…”

supporting

confidence: 54%

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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“…Possibly, rosiglitazone, via its interaction with transcription factor PPARγ, may change the expression of one or several proteins that play a regulatory role in endosomal recycling such as rab, SNARE, or sorting nexin proteins [28,29]. In support of this, the rosiglitazoneinduced effects on GLUT4 required several days of treatment.…”

Section: Discussionmentioning

confidence: 78%

Rosiglitazone increases cell surface GLUT4 levels in 3T3-L1 adipocytes through an enhancement of endosomal recycling

Martinez

Berenguer

Bruce

et al. 2010

Biochemical Pharmacology

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Govers. Rosiglitazone increases cell surface GLUT4 levels in 3T3-L1 adipocytes through an enhancement of endosomal recycling. Biochemical Pharmacology, Elsevier, 2010, 79 (9) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 2 AbstractInsulin induces a translocation of the glucose transporter GLUT4 from intracellular storage compartments towards the cell surface in adipocytes and skeletal muscle cells, allowing the cells to take up glucose. In type 2 diabetes-associated insulin resistance, the efficiency of this process is reduced. The thiazolidinediones, widely prescribed as anti-diabetic therapy, are generally regarded as insulin-sensitizers. The aim of this study was to evaluate the effect of the thiazolidinedione rosiglitazone (BRL 49653) on GLUT4 in adipocytes. When applied during differentiation, rosiglitazone dose dependently augmented GLUT4 expression along with the formation of lipid droplets. Intriguingly, its presence during differentiation led to increases in both cell surface GLUT4 levels and insulin-sensitivity of GLUT4 translocation in mature adipocytes. Treatment of fully differentiated adipocytes with rosiglitazone also led to increases in GLUT4 at the plasma membrane. Rosiglitazone similarly affected cell surface levels of the endosomal transferrin receptor, but did not alter the GLUT4 internalization rate.The augmentation in cell surface GLUT4 levels was maintained in adipocytes that were rendered insulin resistant in vitro by a 24 hour insulin treatment and moreover in these cells rosiglitazone also fully restored insulin-induced GLUT4 translocation. We conclude that in adipocytes, rosiglitazone increases cell surface GLUT4 levels by increasing its endosomal recycling and restores insulin-induced GLUT4 translocation in insulin resistance. These results implicate novel modes of action on GLUT4 that are all likely to contribute to the insulin-sensitizing effect of rosiglitazone in type 2 diabetes.

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Sorting nexin 17 facilitates LRP recycling in the early endosome

Cited by 141 publications

References 38 publications

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

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

Rosiglitazone increases cell surface GLUT4 levels in 3T3-L1 adipocytes through an enhancement of endosomal recycling

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