scispace - formally typeset
Search or ask a question
Topic

Late endosome

About: Late endosome is a research topic. Over the lifetime, 1015 publications have been published within this topic receiving 55419 citations.


Papers
More filters
Journal ArticleDOI
07 Dec 2012-Cell
TL;DR: This work identifies syntaxin 17 (Stx17) as the autophagosomal SNARE required for fusion with the endosome/lysosome, and reveals a mechanism by which the SNARE protein is available to the completed Autophagosome.

988 citations

Journal ArticleDOI
Peter Cresswell1
TL;DR: MHC class II molecules assemble in the endoplasmic reticulum in a chaperone-mediated fashion to form a nine-chain structure consisting of three alpha beta dimers associated with an invariant chain trimer that is transported through the Golgi apparatus and into the endosomal system.
Abstract: MHC class II molecules assemble in the endoplasmic reticulum in a chaperone-mediated fashion to form a nine-chain structure consisting of three alpha beta dimers associated with an invariant chain trimer. This complex is transported through the Golgi apparatus and into the endosomal system. The signal for endosomal targeting resides in the cytoplasmic tail of the invariant chain. Current evidence argues that the segregation of the class II-invariant chain complex from the constitutive pathway of membrane protein transport occurs in the trans-Golgi network. However, class II-invariant chain complexes that reach the cell surface are also rapidly internalized into endosomes. Within the endosomal system, probably in a late endosome/pre-lysosome, the invariant chain is degraded, releasing alpha beta dimers that bind peptides predominantly derived from endocytosed proteins. Evidence suggests that many of these peptides are actually generated in lysosomes. The precise mechanisms involved in forming class II-pept...

851 citations

Journal ArticleDOI
TL;DR: It is shown that Beclin was co‐immunoprecipitated with phosphatidylinositol (PtdIns) 3‐kinase, which is also required for autophagy, suggesting that BeClin is a component of the PtdIns 3‐Kinase complex.
Abstract: Autophagy is an intracellular bulk protein degradation system. Beclin is known to be involved in this process; however, its role is unclear. In this study, we showed that Beclin was co-immunoprecipitated with phosphatidylinositol (PtdIns) 3-kinase, which is also required for autophagy, suggesting that Beclin is a component of the PtdIns 3-kinase complex. Quantitative analyses using a cross-linker showed that all Beclin forms a complex with PtdIns 3-kinase, whereas ∼50% of PtdIns 3-kinase remains free from Beclin. Indirect immunofluorescence microscopy demonstrated that the majority of Beclin and PtdIns 3-kinase localize to the trans-Golgi network (TGN). Some PtdIns 3-kinase is also distributed in the late endosome. These results suggest that Beclin and PtdIns 3-kinase control autophagy as a complex at the TGN.

812 citations

Journal ArticleDOI
TL;DR: It is found that NPC1-mutant cells have a large reduction in the acidic compartment calcium store compared to wild-type cells, which represents a new target for therapeutic intervention, as elevation of cytosolic calcium with curcumin normalized NPC1 disease cellular phenotypes and prolonged survival of the NPC1 mouse.
Abstract: Niemann-Pick type C1 (NPC1) disease is a neurodegenerative lysosomal storage disorder caused by mutations in the acidic compartment (which we define as the late endosome and the lysosome) protein, NPC1. The function of NPC1 is unknown, but when it is dysfunctional, sphingosine, glycosphingolipids, sphingomyelin and cholesterol accumulate. We have found that NPC1-mutant cells have a large reduction in the acidic compartment calcium store compared to wild-type cells. Chelating luminal endocytic calcium in normal cells with high-affinity Rhod-dextran induced an NPC disease cellular phenotype. In a drug-induced NPC disease cellular model, sphingosine storage in the acidic compartment led to calcium depletion in these organelles, which then resulted in cholesterol, sphingomyelin and glycosphingolipid storage in these compartments. Sphingosine storage is therefore an initiating factor in NPC1 disease pathogenesis that causes altered calcium homeostasis, leading to the secondary storage of sphingolipids and cholesterol. This unique calcium phenotype represents a new target for therapeutic intervention, as elevation of cytosolic calcium with curcumin normalized NPC1 disease cellular phenotypes and prolonged survival of the NPC1 mouse.

762 citations

Journal Article
TL;DR: It is demonstrated, after subcellular fractionation procedures, that MDC-labeled organelles contained the lysosomal enzymes acid phosphatase and the mature form of cathepsin D, and Membrane markers of rough endoplasmic reticulum (TRAM and sec61 beta), and for smooth endoplasmsic reticle (cytochrome P450) were not detected in the same fractions.

712 citations


Network Information
Related Topics (5)
Phosphorylation
69.3K papers, 3.8M citations
84% related
Signal transduction
122.6K papers, 8.2M citations
83% related
Kinase
65.8K papers, 3.5M citations
81% related
Regulation of gene expression
85.4K papers, 5.8M citations
81% related
Protein kinase A
68.4K papers, 3.9M citations
81% related
Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20222
202164
202047
201950
201843
201754