A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells

Ganley, Ian G.; Espinosa, Eric J.; Pfeffer, Suzanne R.

doi:10.1083/jcb.200707136

Cited by 164 publications

(198 citation statements)

References 61 publications

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“…4 and 5 and S6), suggesting that more than 1 SNARE complex may be involved in the vesicular transport of LDL-CHOL from the endosomes to the TGN, similarly to what has been demonstrated in protein transport studies (33,43). Assuming nocodazole acts by rapidly disintegrating the TGN, the results presented in Fig.…”

Section: Discussionsupporting

confidence: 64%

Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex

Urano

Watanabe

Murphy

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

106

131

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Mammalian cells acquire cholesterol mainly from LDL. LDL enter the endosomes, allowing cholesteryl esters to be hydrolyzed by acid lipase. The hydrolyzed cholesterol (LDL-CHOL) enters the Niemann–Pick type C1 (NPC1)-containing endosomal compartment en route to various destinations. Whether the Golgi is involved in LDL-CHOL transport downstream of the NPC1 compartment has not been demonstrated. Using subcellular fractionation and immunoadsorption to enrich for specific membrane fractions, here we show that, when parental Chinese hamster ovary (CHO) cells are briefly exposed to 3 H-cholesteryl linoleate (CL) labeled-LDL, newly liberated 3 H-LDL-CHOL appears in membranes rich in trans-Golgi network (TGN) long before it becomes available for re-esterification at the endoplasmic reticulum (ER) or for efflux at the plasma membrane. In mutant cells lacking NPC1, the appearance of newly liberated 3 H-LDL-CHOL in the TGN-rich fractions is much reduced. We next report a reconstituted transport system that recapitulates the transport of LDL-CHOL to the TGN and to the ER. The transport system requires ATP and cytosolic factors and depends on functionality of NPC1. We demonstrate that knockdown by RNAi of 3 TGN-specific SNAREs (VAMP4, syntaxin 6, and syntaxin 16) reduces ≥50% of the LDL-CHOL transport in intact cells and in vitro. These results show that vesicular trafficking is involved in transporting a significant portion of LDL-CHOL from the NPC1-containing endosomal compartment to the TGN before its arrival at the ER.

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Section: Discussionsupporting

confidence: 64%

Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex

Urano

Watanabe

Murphy

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

106

131

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“…In the absence of MPRs lysosomal enzymes follow the default pathway from the TGN to the plasma membrane for secretion (16). Interference with vti1a function results in reduced transport of MPRs from endosomes to the TGN in vitro (10,17) and in increased secretion of lysosomal enzymes (17). We found that DKO fibroblasts secreted almost twice as much lysosomal β-glucuronidase and β-galactosidase normalized to total enzyme content ( Fig.…”

Section: Resultsmentioning

confidence: 57%

“…S9A), even though we did not observe differences in MPR steady-state distribution. Return of MPR to the TGN depends on vti1a and its partner syntaxin16 in vitro (10,17,30).…”

Section: Discussionmentioning

confidence: 99%

Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development

Kunwar

Rickmann²,

Backofen³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Fusion between membranes is mediated by specific SNARE complexes. Here we report that fibroblasts survive the absence of the trans-Golgi network/early endosomal SNARE vti1a and the late endosomal SNARE vti1b with intact organelle morphology and minor trafficking defects. Because vti1a and vti1b are the only members of their SNARE subclass and the yeast homolog Vti1p is essential for cell survival, these data suggest that more distantly related SNAREs acquired the ability to function in endosomal traffic during evolution. However, absence of vti1a and vti1b resulted in perinatal lethality. Major axon tracts were missing, reduced in size, or misrouted in Vti1a −/− Vti1b −/− embryos. Progressive neurodegeneration was observed in most Vti1a −/− Vti1b −/− peripheral ganglia. Neurons were reduced by more than 95% in Vti1a −/− Vti1b −/− dorsal root and geniculate ganglia at embryonic day 18.5. These data suggest that special demands for endosomal membrane traffic could not be met in Vti1a −/− Vti1b −/− neurons. Vti1a −/− and Vti1b −/− single deficient mice were viable without these neuronal defects, indicating that they can substitute for each other in these processes.endosome | neurite outgrowth | neuronal survival

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“…Cargo can be delivered to the TGN from the early endosomes directly by retromer or indirectly by retromer in a Rab7-and Rab9-dependent manner (37,38), routes that TGN46 or CI-M6PR/furin, respectively, employ (38,50). Our study demonstrates conclusively that LGR5 internalizes through Vps26 endosomes with minimal and transient co-localization with Rab7, 9, and 11, leading us to conclude that the bulk of LGR5 likely traffics directly from early endosomes to the TGN following an internalization route more reminiscent of TGN46 than M6PR or furin.…”

Section: Discussionmentioning

confidence: 99%

Constitutive Internalization of the Leucine-rich G Protein-coupled Receptor-5 (LGR5) to the Trans-Golgi Network

Snyder

Rochelle

Lyerly

et al. 2013

Journal of Biological Chemistry

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Background: Expression of the G protein-coupled receptor LGR5 demarcates adult tissue stem cells in the intestine, stomach, hair follicle, and mammary epithelium. Results:LGR5 is rapidly and constitutively internalized to the trans-Golgi network at steady state. Conclusion: Internalization occurs through a potential phosphorylation domain within the C-terminal tail. Significance: An understanding of LGR5 trafficking dynamics is expected to clarify its role in signaling and stem cell biology.

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A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells

Cited by 164 publications

References 61 publications

Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex

Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex

Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development

Constitutive Internalization of the Leucine-rich G Protein-coupled Receptor-5 (LGR5) to the Trans-Golgi Network

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