The luminal domain participates in the endosomal trafficking of the cation-independent mannose 6-phosphate receptor

Waguri, Satoshi; Tomiyama, Yoichiro; Ikeda, Hiroko; Hida, Tatsuhiro; Sakai, Norio; Taniike, Masako; Ebisu, Shigeyuki; Uchiyama, Yasuo

doi:10.1016/j.yexcr.2006.09.024

Cited by 14 publications

(11 citation statements)

References 62 publications

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“…These results suggest that retrograde transport is not generally affected by ArfGAP3 depletion. We found that trafficking of the truncated MPR-tail differs from that of the full-length CIMPR (Figure S2D,E) consistent with previous studies [7]. We analyzed the retrograde transport of GFP-MPR-full by internalizing anti-GFP antibody for 30 min (Figure S2F).…”

Section: Resultssupporting

confidence: 86%

“…Due to the low efficiency of transport of internalized GFP-MPR-full to the Golgi in control cells (Figure S2G), we used U18666A, which causes the accumulation of cholesterol in late endosomes and redistributes CIMPR to endosomal structures [7, 8, 9]. This peripherally localized CIMPR is shifted to the TGN upon cycloheximide treatment [7]. CIMPR was redistributed to the periphery in control and ArfGAP3 knockdown cells in the presence of U18666A (Figure 2H).…”

Section: Resultsmentioning

confidence: 99%

“…Fourth, ArfGAP3 affected transport of full-length CIMPR but not truncated CIMPR lacking the luminal region. Waguri et al [7] proposed that the luminal region of CIMPR has a role in endosomal retention of the receptor. Full-length CIMPR is thought to be transported from early to late endosomes and then returns to the TGN [30], whereas truncated CIMPR is possibly transported from early endosomes to the TGN directly [31].…”

Section: Resultsmentioning

confidence: 99%

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ArfGAP3 Regulates the Transport of Cation-Independent Mannose 6-Phosphate Receptor in the Post-Golgi Compartment

et al. 2013

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Summary ArfGAPs are known to be involved in cargo sorting in COPI transport. However, the role of ArfGAPs in post-Golgi membrane traffic has not been defined. To determine the function of ArfGAPs in post-Golgi traffic, we used siRNA to examine each of 25 ArfGAPs for effects on cation-independent mannose 6-phosphate receptor (CIMPR) localization. We found that down-regulation of ArfGAP3 resulted in the peripheral localization of CIMPR. The effect was specific for ArfGAP3 and dependent on its GAP activity, because the phenotype was rescued by ArfGAP3 but not by ArfGAP1, ArfGAP2 or the GAP domain mutants of ArfGAP3. ArfGAP3 localized to the trans-Golgi network and early endosomes. In cells with reduced expression of ArfGAP3, Cathepsin D maturation was slowed and its secretion was accelerated. Also retrograde transport from the endosomes to the trans-Golgi network of endogenous CIMPR, but not truncated CIMPR lacking the luminal domain, was perturbed in cells with reduced expression of ArfGAP3. Furthermore the exit of epidermal growth factor receptor (EGFR) from the early endosomes and degradation of EGFR after EGF stimulation was slowed in cells with reduced expression of ArfGAP3. ArfGAP3 associates with Golgi-localized, γ-ear-containing, ADP-ribosylation factor binding proteins (GGAs), and ArfGAP3 knockdown reduces membrane association of GGAs. A possible mechanism explaining our results is that ArfGAP3 regulates transport from early endosomes to late endosomes. We suggest a model in which ArfGAP3 regulates Golgi association of GGA clathrin adaptors.

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Section: Resultssupporting

confidence: 86%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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ArfGAP3 Regulates the Transport of Cation-Independent Mannose 6-Phosphate Receptor in the Post-Golgi Compartment

et al. 2013

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“…pcDNA3-RFP-APPL1 (Erdmann et al, 2007) was provided by Pietro De Camilli (Yale University, New Haven, CT). The cDNA for CI-MPR (CI-MPR is also known as IGF2R) (Waguri et al, 2006) was used to prepare pCIpremCherry-CIMPR-full. The cDNA for mouse Vps41 was amplified by PCR and subcloned into pmStr-C1 (Ohbayashi et al, 2012).…”

Section: Plasmidsmentioning

confidence: 99%

Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

Yasuda

Morishita

Fujita

et al. 2015

Journal of Cell Science

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Rab GTPases act as molecular switches regulating various aspects of membrane trafficking. Among them, Rab5 and Rab7 play central roles in the endolysosomal network. Although many effectors downstream of Rab7 have been elucidated, our present understanding of the mechanism regulating Rab7 activity is extremely limited. It has only recently been accepted that Mon1-Ccz1 is a Rab7 guanine nucleotide exchange factor, but the question where Mon1-Ccz1 works with Rab7 is hardly answered. To address what kind of change/switch exists in the regulatory mechanism upstream of Rab7 during the transition from late endosome to lysosome, we examined Rab7 activity in steady-state cells and EGF-induced macropinocytosis using a newly developed FRET sensor. A combination of a Rab7 sensor and confocal FRET imaging techniques revealed that the activation of Rab7 on late endosomes depends on Mon1-Ccz1 and is implicated in late endosome-lysosome fusion. In contrast, Rab7 activity on lysosomes was independent of Mon1-Ccz1 and active Rab7 played a role in perinuclear clustering of lysosomes.

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“…We identified genes regulating the metabolism of PI-4P on the Golgi, PI-3P on early endosomes, PI-3,4,5P 3 on recycling endosomes (Fields et al, 2010) and PI-4,5P 2 and PI-3,4,5P 3 at the plasma membrane (Di Paolo and De Camilli, 2006;Vicinanza et al, 2008). Although we cannot exclude the possibility that our GFP-MPR reporter and the full-length MPR follow slightly different routes (Barbero et al, 2002;Waguri et al, 2006), our screen would be consistent with the recycling of MPRs from early endosomes to the TGN, possibly along a retromer-dependent (Arighi et al, 2004;Lin et al, 2004;McKenzie et al, 2012;Popoff et al, 2007;Wassmer et al, 2007) or an AP-1-dependent (Hirst et al, 2012;Meyer et al, 2000) sorting pathway.…”

Section: Discussionmentioning

confidence: 99%

A high throughput siRNA screen identifies genes that regulate mannose 6-phosphate receptor trafficking

Anitei

Ramu

Czupalla

et al. 2014

Journal of Cell Science

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The delivery of newly synthesized soluble lysosomal hydrolases to the endosomal system is essential for lysosome function and cell homeostasis. This process relies on the proper trafficking of the mannose 6-phosphate receptors (MPRs) between the trans-Golgi network (TGN), endosomes and the plasma membrane. Many transmembrane proteins regulating diverse biological processes ranging from virus production to the development of multicellular organisms also use these pathways. To explore how cell signaling modulates MPR trafficking, we used high-throughput RNA interference (RNAi) to target the human kinome and phosphatome. Using high-content image analysis, we identified 127 kinases and phosphatases belonging to different signaling networks that regulate MPR trafficking and/or the dynamic states of the subcellular compartments encountered by the MPRs. Our analysis maps the MPR trafficking pathways based on enzymes regulating phosphatidylinositol phosphate metabolism. Furthermore, it reveals how cell signaling controls the biogenesis of post-Golgi tubular carriers destined to enter the endosomal system through a SRCdependent pathway regulating ARF1 and RAC1 signaling and myosin II activity.

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The luminal domain participates in the endosomal trafficking of the cation-independent mannose 6-phosphate receptor

Cited by 14 publications

References 62 publications

ArfGAP3 Regulates the Transport of Cation-Independent Mannose 6-Phosphate Receptor in the Post-Golgi Compartment

ArfGAP3 Regulates the Transport of Cation-Independent Mannose 6-Phosphate Receptor in the Post-Golgi Compartment

Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

A high throughput siRNA screen identifies genes that regulate mannose 6-phosphate receptor trafficking

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