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Article ; Online: Gold Particle Analyser: Detection and quantitative assessment of electron microscopy gold probes.

Burgoyne, Thomas / Futter, Clare E

2023 Volume 18, Issue 7, Page(s) e0288811

Abstract: Gold particle probes are an essential electron microscopy tool to examine protein localisation, as well as protein trafficking. They can be introduced into living cells when conjugated to a protein that is endocytosed or to an antibody against a cell ... ...

Abstract	Gold particle probes are an essential electron microscopy tool to examine protein localisation, as well as protein trafficking. They can be introduced into living cells when conjugated to a protein that is endocytosed or to an antibody against a cell surface protein. Alternatively, gold particles can be introduced into fixed cells or tissue when conjugated to antibodies, immunoglobulin binding molecules or chemical probes applied to permeabilised samples or electron microscopy sections. Colloidal gold particles that have not been enlarged through chemical (gold or silver) enhancement are typically spherical and can be prepared in a range of specific sizes, allowing multiple proteins to be localised within a single sample. The typically homogeneous shape and size of the colloidal gold makes them ideal for computer assisted detection and analysis. Here we demonstrate a program developed to automatically identify two sizes of gold particle and perform a range of analyses that includes (i) distribution and cluster analysis; (ii) selection and analysis of gold particles allocated close to or either side of a membrane; (iii) measurement of organelle size; (iv) estimation of the number of gold particles within an aggregate and (v) the detection of chemically enhanced irregular sized and shaped gold particles. We show this easy-to-use program can greatly assist electron microscopists, to reliably and efficiently analyse gold particles within their images.
MeSH term(s)	Immunohistochemistry ; Microscopy, Electron ; Silver ; Gold Colloid/analysis ; Antibodies
Chemical Substances	Silver (3M4G523W1G) ; Gold Colloid ; Antibodies
Language	English
Publishing date	2023-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0288811
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Article ; Online: Membrane trafficking: Retrofusion as an escape route out of the endosome.

Eden, Emily R / Futter, Clare E

Current biology : CB

2021 Volume 31, Issue 17, Page(s) R1037–R1040

Abstract: Intraluminal vesicles accumulate within the endosomal lumen before lysosomal delivery or extracellular release. A new study reports the development of an elegant assay showing that these vesicles can escape from the endosomal lumen by 'back-fusion' or ' ... ...

Abstract	Intraluminal vesicles accumulate within the endosomal lumen before lysosomal delivery or extracellular release. A new study reports the development of an elegant assay showing that these vesicles can escape from the endosomal lumen by 'back-fusion' or 'retrofusion' with the endosomal limiting membrane.
MeSH term(s)	Endosomes ; Intracellular Membranes ; Lysosomes
Language	English
Publishing date	2021-09-13
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2021.07.055
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Zs.A 3208: Show issues

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Article ; Online: Membrane trafficking in the retinal pigment epithelium at a glance.

Storm, Tina / Burgoyne, Thomas / Futter, Clare E

Journal of cell science

2020 Volume 133, Issue 16

Abstract: The retinal pigment epithelium (RPE) is a highly specialised pigmented monolayer sandwiched between the choroid and the photoreceptors in the retina. Key functions of the RPE include transport of nutrients to the neural retina, removal of waste products ... ...

Abstract	The retinal pigment epithelium (RPE) is a highly specialised pigmented monolayer sandwiched between the choroid and the photoreceptors in the retina. Key functions of the RPE include transport of nutrients to the neural retina, removal of waste products and water from the retina to the blood, recycling of retinal chromophores, absorption of scattered light and phagocytosis of the tips of the photoreceptor outer segments. These functions place a considerable membrane trafficking burden on the RPE. In this Cell Science at a Glance article and the accompanying poster, we focus on RPE-specific adaptations of trafficking pathways. We outline mechanisms underlying the polarised expression of membrane proteins, melanosome biogenesis and movement, and endocytic trafficking, as well as photoreceptor outer segment phagocytosis and degradation. We also briefly discuss theories of how dysfunction in trafficking pathways contributes to retinal disease.
MeSH term(s)	Humans ; Membrane Proteins ; Phagocytosis ; Retina ; Retinal Diseases ; Retinal Pigment Epithelium
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2020-08-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.238279
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Article ; Online: Changes in Mitochondrial Size and Morphology in the RPE and Photoreceptors of the Developing and Ageing Zebrafish.

Burgoyne, Thomas / Toms, Maria / Way, Chris / Tracey-White, Dhani / Futter, Clare E / Moosajee, Mariya

Cells

2022 Volume 11, Issue 22

Abstract: Mitochondria are essential adenosine triphosphate (ATP)-generating cellular organelles. In the retina, they are highly numerous in the photoreceptors and retinal pigment epithelium (RPE) due to their high energetic requirements. Fission and fusion of the ...

Abstract	Mitochondria are essential adenosine triphosphate (ATP)-generating cellular organelles. In the retina, they are highly numerous in the photoreceptors and retinal pigment epithelium (RPE) due to their high energetic requirements. Fission and fusion of the mitochondria within these cells allow them to adapt to changing demands over the lifespan of the organism. Using transmission electron microscopy, we examined the mitochondrial ultrastructure of zebrafish photoreceptors and RPE from 5 days post fertilisation (dpf) through to late adulthood (3 years). Notably, mitochondria in the youngest animals were large and irregular shaped with a loose cristae architecture, but by 8 dpf they had reduced in size and expanded in number with more defined cristae. Investigation of temporal gene expression of several mitochondrial-related markers indicated fission as the dominant mechanism contributing to the changes observed over time. This is likely to be due to continued mitochondrial stress resulting from the oxidative environment of the retina and prolonged light exposure. We have characterised retinal mitochondrial ageing in a key vertebrate model organism, that provides a basis for future studies of retinal diseases that are linked to mitochondrial dysfunction.
MeSH term(s)	Animals ; Retinal Pigment Epithelium/metabolism ; Mitochondrial Size ; Zebrafish ; Retina/physiology ; Aging
Language	English
Publishing date	2022-11-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11223542
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Article ; Online: Impaired Lysosome Reformation in Chloroquine-Treated Retinal Pigment Epithelial Cells.

Cardoso, M Helena / Hall, Michael J / Burgoyne, Thomas / Fale, Pedro / Storm, Tina / Escrevente, Cristina / Antas, Pedro / Seabra, Miguel C / Futter, Clare E

Investigative ophthalmology & visual science

2023 Volume 64, Issue 11, Page(s) 10

Abstract: Purpose: To model the in vivo effects of chloroquine on the retinal pigment epithelium in experimentally tractable cell culture systems and determine the effects of mild chloroquine treatment on lysosome function and turnover.: Methods: Effects of ... ...

Abstract	Purpose: To model the in vivo effects of chloroquine on the retinal pigment epithelium in experimentally tractable cell culture systems and determine the effects of mild chloroquine treatment on lysosome function and turnover. Methods: Effects of low-dose chloroquine treatment on lysosomal function and accessibility to newly endocytosed cargo were investigated in primary and embryonic stem cell-derived RPE cells and ARPE19 cells using fluorescence and electron microscopy of fluorescent and gold-labeled probes. Lysosomal protein expression and accumulation were measured by quantitative PCR and Western blotting. Results: Initial chloroquine-induced lysosome neutralization was followed by partial recovery, lysosomal expansion, and accumulation of undegraded endocytic, phagocytic, and autophagic cargo and inhibition of cathepsin D processing. Accumulation of enlarged lysosomes was accompanied by a gradual loss of accessibility of these structures to the endocytic pathway, implying impaired lysosome reformation. Chloroquine-induced accumulation of pro-cathepsin D, as well as the lysosomal membrane protein, LAMP1, was reproduced by treatment with protease inhibitors and preceded changes in lysosomal gene expression. Conclusions: Low-dose chloroquine treatment inhibits lysosome reformation, causing a gradual depletion of lysosomes able to interact with cargo-carrying vacuoles and degrade their content. The resulting accumulation of newly synthesized pro-cathepsin D and LAMP1 reflects inhibition of normal turnover of lysosomal constituents and possibly lysosomes themselves. A better understanding of the mechanisms underlying lysosome reformation may reveal new targets for the treatment of chloroquine-induced retinopathy.
MeSH term(s)	Humans ; Chloroquine/toxicity ; Lysosomes/metabolism ; Phagocytosis ; Autophagy/physiology ; Retinal Diseases/metabolism ; Epithelial Cells/metabolism ; Retinal Pigments/metabolism
Chemical Substances	Chloroquine (886U3H6UFF) ; Retinal Pigments
Language	English
Publishing date	2023-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	391794-0
ISSN	1552-5783 ; 0146-0404
ISSN (online)	1552-5783
ISSN	0146-0404
DOI	10.1167/iovs.64.11.10
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Zs.A 45: Show issues

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Article ; Online: Coming or going? Un-BLOC-ing delivery and recycling pathways during melanosome maturation.

Futter, Clare E / Cutler, Daniel F

The Journal of cell biology

2016 Volume 214, Issue 3, Page(s) 245–247

Abstract: Melanosome biogenesis requires successive waves of cargo delivery from endosomes to immature melanosomes, coupled with recycling of the trafficking machinery. Dennis et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201605090) report differential ...

Abstract	Melanosome biogenesis requires successive waves of cargo delivery from endosomes to immature melanosomes, coupled with recycling of the trafficking machinery. Dennis et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201605090) report differential roles for BLOC-1 and BLOC-3 complexes in delivery and recycling of melanosomal biogenetic components, supplying directionality to melanosome maturation.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Cell Differentiation ; Endocytosis ; Endosomes/metabolism ; Humans ; Melanosomes/metabolism ; Models, Biological
Chemical Substances	Carrier Proteins
Language	English
Publishing date	2016-07-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201607023
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Article ; Online: Stress reveals new destination for EGF receptor.

Tomas, Alejandra / Futter, Clare E

Cell cycle (Georgetown, Tex.)

2015 Volume 14, Issue 21, Page(s) 3343–3344

MeSH term(s)	DNA-Binding Proteins/metabolism ; Endocytosis ; Endosomal Sorting Complexes Required for Transport/metabolism ; ErbB Receptors/metabolism ; Humans ; Microfilament Proteins/metabolism ; Transcription Factors/metabolism
Chemical Substances	DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport ; Microfilament Proteins ; Transcription Factors ; ErbB Receptors (EC 2.7.10.1)
Language	English
Publishing date	2015-09-29
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.1080/15384101.2015.1093432
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Zs.A 5881: Show issues

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Article ; Online: Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation.

Wong, Louise H / Eden, Emily R / Futter, Clare E

Biochemical Society transactions

2018 Volume 46, Issue 5, Page(s) 1055–1062

Abstract: Multivesicular endosomes/bodies (MVBs) sort membrane proteins between recycling and degradative pathways. Segregation of membrane proteins onto intraluminal vesicles (ILVs) of MVBs removes them from the recycling pathway and facilitates their degradation ...

Abstract	Multivesicular endosomes/bodies (MVBs) sort membrane proteins between recycling and degradative pathways. Segregation of membrane proteins onto intraluminal vesicles (ILVs) of MVBs removes them from the recycling pathway and facilitates their degradation following fusion of MVBs with lysosomes. Sorting of many cargos onto ILVs depends on the ESCRT (Endosomal Sorting Complex Required for Transport) machinery, although ESCRT-independent mechanisms also exist. In mammalian cells, efficient sorting of ligand-stimulated epidermal growth factor receptors onto ILVs also depends on the tyrosine phosphatase, PTP1B, an ER-localised enzyme that interacts with endosomal targets at membrane contacts between MVBs and the ER. This review focuses on the potential roles played by ER:MVB membrane contact sites in regulating ESCRT-dependent ILV formation.
MeSH term(s)	Annexin A1/metabolism ; Cholesterol/metabolism ; Cytoplasm/metabolism ; Endocytosis ; Endoplasmic Reticulum/metabolism ; Endosomal Sorting Complexes Required for Transport/metabolism ; Endosomes/metabolism ; Epidermal Growth Factor/metabolism ; ErbB Receptors/metabolism ; HeLa Cells ; Humans ; Lysosomes/metabolism ; Mitochondrial Membranes/metabolism ; Multivesicular Bodies ; Phosphorylation ; Protein Binding ; Protein Transport ; Protein Tyrosine Phosphatase, Non-Receptor Type 1/metabolism
Chemical Substances	Annexin A1 ; Endosomal Sorting Complexes Required for Transport ; Epidermal Growth Factor (62229-50-9) ; Cholesterol (97C5T2UQ7J) ; ErbB Receptors (EC 2.7.10.1) ; PTPN1 protein, human (EC 3.1.3.48) ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 (EC 3.1.3.48)
Language	English
Publishing date	2018-09-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20170432
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Zs.A 944: Show issues

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Article ; Online: Chronically shortened rod outer segments accompany photoreceptor cell death in Choroideremia.

Meschede, Ingrid P / Burgoyne, Thomas / Tolmachova, Tanya / Seabra, Miguel C / Futter, Clare E

PloS one

2020 Volume 15, Issue 11, Page(s) e0242284

Abstract: X-linked choroideremia (CHM) is a disease characterized by gradual retinal degeneration caused by loss of the Rab Escort Protein, REP1. Despite partial compensation by REP2 the disease is characterized by prenylation defects in multiple members of the ... ...

Abstract	X-linked choroideremia (CHM) is a disease characterized by gradual retinal degeneration caused by loss of the Rab Escort Protein, REP1. Despite partial compensation by REP2 the disease is characterized by prenylation defects in multiple members of the Rab protein family that are master regulators of membrane traffic. Remarkably, the eye is the only organ affected in CHM patients, possibly because of the huge membrane traffic burden of the post mitotic photoreceptors, which synthesise outer segments, and the adjacent retinal pigment epithelium that degrades the spent portions each day. In this study, we aimed to identify defects in membrane traffic that might lead to photoreceptor cell death in CHM. In a heterozygous null female mouse model of CHM (Chmnull/WT), degeneration of the photoreceptor layer was clearly evident from increased numbers of TUNEL positive cells compared to age matched controls, small numbers of cells exhibiting signs of mitochondrial stress and greatly increased microglial infiltration. However, most rod photoreceptors exhibited remarkably normal morphology with well-formed outer segments and no discernible accumulation of transport vesicles in the inner segment. The major evidence of membrane trafficking defects was a shortening of rod outer segments that was evident at 2 months of age but remained constant over the period during which the cells die. A decrease in rhodopsin density found in the outer segment may underlie the outer segment shortening but does not lead to rhodopsin accumulation in the inner segment. Our data argue against defects in rhodopsin transport or outer segment renewal as triggers of cell death in CHM.
MeSH term(s)	Adaptor Proteins, Signal Transducing/deficiency ; Adaptor Proteins, Signal Transducing/genetics ; Animals ; Apoptosis ; Choroideremia/metabolism ; Choroideremia/pathology ; Disease Models, Animal ; Female ; Mice ; Mice, Knockout ; Microscopy, Electron, Transmission ; Mitochondria/metabolism ; Photoreceptor Cells, Vertebrate/metabolism ; Photoreceptor Cells, Vertebrate/ultrastructure ; Rhodopsin/metabolism ; Rod Cell Outer Segment/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Chm protein, mouse ; Rhodopsin (9009-81-8)
Language	English
Publishing date	2020-11-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0242284
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Article ; Online: Cholesterol Overload: Contact Sites to the Rescue!

Enrich, Carlos / Rentero, Carles / Grewal, Thomas / Futter, Clare E / Eden, Emily R

Contact (Thousand Oaks (Ventura County, Calif.))

2019 Volume 2, Page(s) 2515256419893507

Abstract: Delivery of low-density lipoprotein-derived cholesterol to the endoplasmic reticulum (ER) is essential for cholesterol homeostasis, yet the mechanism of this transport has largely remained elusive. Two recent reports shed some light on this process, ... ...

Abstract	Delivery of low-density lipoprotein-derived cholesterol to the endoplasmic reticulum (ER) is essential for cholesterol homeostasis, yet the mechanism of this transport has largely remained elusive. Two recent reports shed some light on this process, uncovering a role for Niemann Pick type-C1 protein (NPC1) in the formation of membrane contact sites (MCS) between late endosomes (LE)/lysosomes (Lys) and the ER. Both studies identified a loss of MCS in cells lacking functional NPC1, where cholesterol accumulates in late endocytic organelles. Remarkably, and taking different approaches, both studies have made a striking observation that expansion of LE/Lys-ER MCS can rescue the cholesterol accumulation phenotype in NPC1 mutant or deficient cells. In both cases, the cholesterol was shown to be transported to the ER, demonstrating the importance of ER-LE/Lys contact sites in the direct transport of low-density lipoprotein-derived cholesterol to the ER.
Language	English
Publishing date	2019-12-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/2515256419893507
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