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Article ; Online: Targeting Recycling Endosomes to Potentiate mRNA Lipid Nanoparticles.

Shin, Jeehae / Douglas, Cameron J / Zhang, Shanwen / Seath, Ciaran P / Bao, Huan

Nano letters

2024 Volume 24, Issue 17, Page(s) 5104–5109

Abstract: ... molecules, endosidine 5 (ES5), interferes with recycling endosomes through Annexin A6, thereby promoting ... enhanced via inhibition of endocytic recycling in cells and in live mice. One of the most potent small ... few decades, endosomal entrapment of delivered mRNAs vastly impedes therapeutic developments. In addition ...

Abstract	mRNA lipid nanoparticles (LNPs) have emerged as powerful modalities for gene therapies to control cancer and infectious and immune diseases. Despite the escalating interest in mRNA-LNPs over the past few decades, endosomal entrapment of delivered mRNAs vastly impedes therapeutic developments. In addition, the molecular mechanism of LNP-mediated mRNA delivery is poorly understood to guide further improvement through rational design. To tackle these challenges, we characterized LNP-mediated mRNA delivery using a library of small molecules targeting endosomal trafficking. We found that the expression of delivered mRNAs is greatly enhanced via inhibition of endocytic recycling in cells and in live mice. One of the most potent small molecules, endosidine 5 (ES5), interferes with recycling endosomes through Annexin A6, thereby promoting the release and expression of mRNA into the cytoplasm. Together, these findings suggest that targeting endosomal trafficking with small molecules is a viable strategy to potentiate the efficacy of mRNA-LNPs.
MeSH term(s)	Endosomes/metabolism ; Animals ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Nanoparticles/chemistry ; Mice ; Humans ; Lipids/chemistry ; Gene Transfer Techniques ; Endocytosis/drug effects ; Liposomes
Chemical Substances	RNA, Messenger ; Lipids ; Lipid Nanoparticles ; Liposomes
Language	English
Publishing date	2024-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ISSN	1530-6992
ISSN (online)	1530-6992
DOI	10.1021/acs.nanolett.3c04415
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Article: A Role of Phosphatidylserine in the Function of Recycling Endosomes.

Hasegawa, Junya / Uchida, Yasunori / Mukai, Kojiro / Lee, Shoken / Matsudaira, Tatsuyuki / Taguchi, Tomohiko

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 783857

Abstract: ... of proteins and lipids to PM through recycling pathway. Recycling endosomes (REs) are specific subsets ... of endosomes. Besides the established role of REs in recycling pathway, recent studies have revealed ...

Abstract	Cells internalize proteins and lipids in the plasma membrane (PM) and solutes in the extracellular space by endocytosis. The removal of PM by endocytosis is constantly balanced by the replenishment of proteins and lipids to PM through recycling pathway. Recycling endosomes (REs) are specific subsets of endosomes. Besides the established role of REs in recycling pathway, recent studies have revealed unanticipated roles of REs in membrane traffic and cell signalling. In this review, we highlight these emerging issues, with a particular focus on phosphatidylserine (PS), a phospholipid that is highly enriched in the cytosolic leaflet of RE membranes. We also discuss the pathogenesis of Hermansky Pudlak syndrome type 2 (HPS2) that arises from mutations in the AP3B1 gene, from the point of view of dysregulated RE functions.
Language	English
Publishing date	2021-12-24
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.783857
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Article ; Online: Mammalian phagophores with finger-like shapes emerge from recycling endosomes.

Puri, Claudia / Rubinsztein, David C

Autophagy

2023 Volume 20, Issue 5, Page(s) 1189–1191

Abstract: ... from the recycling endosomes liberates free autophagosomes from this compartment. These data reveal unexpected ... derive from finger-like outgrowths from the recycling endosome. These "fingers" survey a large ... while the precursors are still attached to the recycling endosome. We call this transient recycling endosome-attached ...

Abstract	Autophagosomes are double-membraned vesicles that engulf cytoplasmic contents, which are ultimately degraded after autophagosome-lysosome fusion. The prevailing view, largely inferred from EM-based studies, was that mammalian autophagosomes evolved from disc-shaped precursors that invaginated and then were closed at the single opening. Many site(s) of origin of these precursors have been proposed. Using superresolution structured illumination microscopy and electron microscopy, we find that mammalian autophagosomes derive from finger-like outgrowths from the recycling endosome. These "fingers" survey a large cell volume and then close into a "fist" and the openings are sealed in an ESCRT-dependent fashion, while the precursors are still attached to the recycling endosome. We call this transient recycling endosome-attached, closed, autophagic structure an "autophago-dome". DNM2-dependent scission of the autophago-dome from the recycling endosomes liberates free autophagosomes from this compartment. These data reveal unexpected morphologies of autophagosome precursors and raise new questions about the control of this process.
MeSH term(s)	Endosomes/metabolism ; Autophagosomes/metabolism ; Animals ; Humans ; Autophagy/physiology ; Mammals/metabolism ; Phagosomes/metabolism ; Phagosomes/ultrastructure ; HeLa Cells ; Endosomal Sorting Complexes Required for Transport/metabolism ; Lysosomes/metabolism
Chemical Substances	Endosomal Sorting Complexes Required for Transport
Language	English
Publishing date	2023-12-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2023.2293439
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Article ; Online: Kazrin promotes dynein/dynactin-dependent traffic from early to recycling endosomes.

Hernandez-Perez, Ines / Rubio, Javier / Baumann, Adrian / Girao, Henrique / Ferrando, Miriam / Rebollo, Elena / Aragay, Anna M / Geli, María Isabel

eLife

2023 Volume 12

Abstract: ... to recycling endosomes. Consistently, we found that the C-terminal domain of kazrin C, predicted to be ... of EEs or EE-derived transport intermediates to the recycling endosomes. ... kazrin functions is to facilitate endocytic recycling by promoting dynein/dynactin-dependent transport ...

Abstract	Kazrin is a protein widely expressed in vertebrates whose depletion causes a myriad of developmental defects, in part derived from altered cell adhesion and migration, as well as failure to undergo epidermal to mesenchymal transition. However, the primary molecular role of kazrin, which might contribute to all these functions, has not been elucidated yet. We previously identified one of its isoforms, kazrin C, as a protein that potently inhibits clathrin-mediated endocytosis when overexpressed. We now generated kazrin knock-out mouse embryonic fibroblasts to investigate its endocytic function. We found that kazrin depletion delays juxtanuclear enrichment of internalized material, indicating a role in endocytic traffic from early to recycling endosomes. Consistently, we found that the C-terminal domain of kazrin C, predicted to be an intrinsically disordered region, directly interacts with several early endosome (EE) components, and that kazrin depletion impairs retrograde motility of these organelles. Further, we noticed that the N-terminus of kazrin C shares homology with dynein/dynactin adaptors and that it directly interacts with the dynactin complex and the dynein light intermediate chain 1. Altogether, the data indicate that one of the primary kazrin functions is to facilitate endocytic recycling by promoting dynein/dynactin-dependent transport of EEs or EE-derived transport intermediates to the recycling endosomes.
MeSH term(s)	Animals ; Mice ; Dynactin Complex/metabolism ; Dyneins/metabolism ; Endosomes/metabolism ; Fibroblasts/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism
Chemical Substances	Dynactin Complex ; Dyneins (EC 3.6.4.2) ; Microtubule-Associated Proteins ; Kazn protein, mouse
Language	English
Publishing date	2023-04-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.83793
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Article ; Online: LRBA signalosomes activate vasopressin-induced AQP2 trafficking at recycling endosomes.

Yanagawa, Hideki / Hara, Yu / Ando, Fumiaki / Suzuki, Soichiro / Fujiki, Tamami / Oikawa, Daisuke / Yui, Naofumi / Mandai, Shintaro / Mori, Yutaro / Susa, Koichiro / Mori, Takayasu / Sohara, Eisei / Tokunaga, Fuminori / Uchida, Shinichi

The Journal of physiology

2023 Volume 601, Issue 23, Page(s) 5437–5451

Abstract: ... immunoelectron microscopy. Most of the AQP2 was localized on the recycling endosome in the presence of tolvaptan ... it from the recycling endosome to the apical plasma membrane. In contrast, LRBA was constitutively localized ... at the recycling endosome. Therefore, LRBA and AQP2 were well colocalized in the absence of vasopressin stimulation ...

Abstract	Aquaporin-2 (AQP2) water channels are proteins that are recycled between intracellular vesicles and the apical plasma membrane in renal collecting ducts. Lipopolysaccharide-responsive beige-like anchor protein (LRBA) is a protein kinase A (PKA) anchoring protein that creates compartmentalized PKA signalling responsible for AQP2 phosphorylation. In response to increased plasma osmolality, vasopressin/cyclic adenosine monophosphate (cAMP)/PKA signalling phosphorylates AQP2, promoting AQP2 trafficking into the apical plasma membrane and increasing water reabsorption from urine. However, the molecular mechanisms by which LRBA mediates vasopressin-induced AQP2 phosphorylation remain unknown. To investigate AQP2 intracellular localization and phosphorylation status in vivo, a density gradient ultracentrifugation technique was combined with an in situ proximity ligation assay, super-resolution structured illumination microscopy and immunoelectron microscopy. Most of the AQP2 was localized on the recycling endosome in the presence of tolvaptan, a vasopressin type 2 receptor (V2R) antagonist. Desmopressin, a V2R agonist, phosphorylated AQP2, translocating it from the recycling endosome to the apical plasma membrane. In contrast, LRBA was constitutively localized at the recycling endosome. Therefore, LRBA and AQP2 were well colocalized in the absence of vasopressin stimulation. The loss of LRBA/PKA signalling by Lrba knockout impaired vasopressin-induced AQP2 phosphorylation, resulting in AQP2 retention at the recycling endosome. Defective AQP2 trafficking caused low urinary concentrating ability in Lrba
MeSH term(s)	Mice ; Animals ; Aquaporin 2/metabolism ; CTLA-4 Antigen/metabolism ; Lipopolysaccharides/metabolism ; Protein Transport ; Vasopressins/pharmacology ; Vasopressins/metabolism ; Endosomes/metabolism ; Antidiuretic Hormone Receptor Antagonists ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Water/metabolism ; Phosphorylation ; Kidney Tubules, Collecting
Chemical Substances	Aquaporin 2 ; CTLA-4 Antigen ; Lipopolysaccharides ; Vasopressins (11000-17-2) ; Antidiuretic Hormone Receptor Antagonists ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Water (059QF0KO0R)
Language	English
Publishing date	2023-10-20
Publishing country	England
Document type	Journal Article
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/JP285188
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Uc I Zs.65: Show issues

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Article ; Online: Recycling endosomes.

Goldenring, James R

Current opinion in cell biology

2015 Volume 35, Page(s) 117–122

Abstract: ... internalized membrane constituents. The recycling system is composed of multiple tubulovesicular recycling ... cilia and apical microvilli. The existence of multiple intersecting and diverging recycling tracks ... likely accounts for specificity in plasma membrane recycling trafficking. ...

Abstract	The endosomal membrane recycling system represents a dynamic conduit for sorting and re-exporting internalized membrane constituents. The recycling system is composed of multiple tubulovesicular recycling pathways that likely confer distinct trafficking pathways for individual cargoes. In addition, elements of the recycling system are responsible for assembly and maintenance of apical membrane specializations including primary cilia and apical microvilli. The existence of multiple intersecting and diverging recycling tracks likely accounts for specificity in plasma membrane recycling trafficking.
MeSH term(s)	Biological Transport ; Cell Membrane/metabolism ; Cell Polarity ; Endocytosis ; Endosomes/chemistry ; Endosomes/metabolism ; Humans
Language	English
Publishing date	2015-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2015.04.018
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Zs.A 2963: Show issues

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Article ; Online: EFA6A, an Exchange Factor for Arf6, Regulates NGF-Dependent TrkA Recycling From Early Endosomes and Neurite Outgrowth in PC12 Cells.

Fukaya, Masahiro / Ibuchi, Kanta / Sugawara, Takeyuki / Itakura, Makoto / Ito, Akiko / Shiroshima, Tomoko / Hara, Yoshinobu / Okamoto, Hirotsugu / Luton, Frédéric / Sakagami, Hiroyuki

Traffic (Copenhagen, Denmark)

2024 Volume 25, Issue 5, Page(s) e12936

Abstract: ... cells and that knockdown of EFA6A significantly inhibited NGF-dependent Arf6 activation, TrkA recycling ... from early endosomes to the cell surface, prolonged ERK1/2 phosphorylation, and neurite outgrowth. We also ... Endosomal trafficking of TrkA is a critical process for nerve growth factor (NGF)-dependent ...

Abstract	Endosomal trafficking of TrkA is a critical process for nerve growth factor (NGF)-dependent neuronal cell survival and differentiation. The small GTPase ADP-ribosylation factor 6 (Arf6) is implicated in NGF-dependent processes in PC12 cells through endosomal trafficking and actin cytoskeleton reorganization. However, the regulatory mechanism for Arf6 in NGF signaling is largely unknown. In this study, we demonstrated that EFA6A, an Arf6-specific guanine nucleotide exchange factor, was abundantly expressed in PC12 cells and that knockdown of EFA6A significantly inhibited NGF-dependent Arf6 activation, TrkA recycling from early endosomes to the cell surface, prolonged ERK1/2 phosphorylation, and neurite outgrowth. We also demonstrated that EFA6A forms a protein complex with TrkA through its N-terminal region, thereby enhancing its catalytic activity for Arf6. Similarly, we demonstrated that EFA6A forms a protein complex with TrkA in cultured dorsal root ganglion (DRG) neurons. Furthermore, cultured DRG neurons from EFA6A knockout mice exhibited disturbed NGF-dependent TrkA trafficking compared with wild-type neurons. These findings provide the first evidence for EFA6A as a key regulator of NGF-dependent TrkA trafficking and signaling.
MeSH term(s)	Animals ; PC12 Cells ; ADP-Ribosylation Factor 6 ; Receptor, trkA/metabolism ; Nerve Growth Factor/metabolism ; Rats ; Endosomes/metabolism ; ADP-Ribosylation Factors/metabolism ; ADP-Ribosylation Factors/genetics ; Neuronal Outgrowth ; Guanine Nucleotide Exchange Factors/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Mice ; Protein Transport ; Ganglia, Spinal/metabolism ; Mice, Knockout
Chemical Substances	ADP-Ribosylation Factor 6 ; Receptor, trkA (EC 2.7.10.1) ; Nerve Growth Factor (9061-61-4) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; Arf6 protein, rat (EC 3.6.5.2) ; Guanine Nucleotide Exchange Factors ; Arf6 protein, mouse (EC 3.6.5.2)
Language	English
Publishing date	2024-05-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12936
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Zs.A 5634: Show issues

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Article ; Online: Phagophores evolve from recycling endosomes.

Puri, Claudia / Vicinanza, Mariella / Rubinsztein, David C

Autophagy

2018 Volume 14, Issue 8, Page(s) 1475–1477

Abstract: ... coincident detection of PtdIns3P and RAB11A, a protein that marks recycling endosomes. We found that multiple ... than with endoplasmic reticulum (ER)-mitochondrial contact sites. Furthermore, biochemical isolation of the recycling endosomes ... that recycling endosomes engulf autophagic substrates. Indeed, the sequestration of mitochondria after mitophagy ...

Abstract	The membrane origins of autophagosomes have been a key unresolved question in the field. The earliest morphologically recognizable structure in the macroautophagy/autophagy itinerary is the double-membraned cup-shaped phagophore. Newly formed phosphatidylinositol 3-phosphate (PtdIns3P) on the membranes destined to become phagophores recruits WIPI2, which, in turn, binds ATG16L1 to define the sites of autophagosome formation. Here we review our recent study showing that membrane recruitment of WIPI2 requires coincident detection of PtdIns3P and RAB11A, a protein that marks recycling endosomes. We found that multiple core autophagy proteins are more tightly associated with the recycling endosome compartment than with endoplasmic reticulum (ER)-mitochondrial contact sites. Furthermore, biochemical isolation of the recycling endosomes confirmed that they recruit autophagy proteins. Finally, fixed and live-cell imaging data revealed that recycling endosomes engulf autophagic substrates. Indeed, the sequestration of mitochondria after mitophagy stimulation depends on early autophagy regulators. These data suggest that autophagosomes evolve from the RAB11A compartment.
MeSH term(s)	Autophagosomes ; Autophagy ; Carrier Proteins ; Endosomes ; Membrane Proteins ; Protein Transport
Chemical Substances	Carrier Proteins ; Membrane Proteins
Language	English
Publishing date	2018-07-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2018.1482148
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Article: Adaptin' endosomes for synaptic vesicle recycling, learning and memory

Haucke, Volker

The EMBO journal, 29: 1313-1315

2010

Abstract: ... provides novel insights into the role of clathrin/AP-1 coats in SV recycling from endosomes, but also ... an unanticipated role for the clathrin adaptor AP-1 and in particular its σ1B subunit in SV recycling. SV ... The pathways by which neurotransmitter-filled presynaptic vesicles (SVs) are generated and recycled ...

Institution	Leibniz-Institut für Molekulare Pharmakologie
Abstract	The pathways by which neurotransmitter-filled presynaptic vesicles (SVs) are generated and recycled have been debated for a long time. Glyvuk et al (2010) in this issue of The EMBO Journal describe an unanticipated role for the clathrin adaptor AP-1 and in particular its σ1B subunit in SV recycling. SV reformation is defective in σ1B-deficient mice, which instead accumulate large endosomelike vacuoles. These defects are paired with reduced motor coordination and long-term spatial memory. This work thus not only provides novel insights into the role of clathrin/AP-1 coats in SV recycling from endosomes, but also unravels a molecular mechanism that may contribute to some forms of X-linked mental retardation.
Language	English
Document type	Article
Database	Repository for Life Sciences

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Article ; Online: A Role of Phosphatidylserine in the Function of Recycling Endosomes

Junya Hasegawa / Yasunori Uchida / Kojiro Mukai / Shoken Lee / Tatsuyuki Matsudaira / Tomohiko Taguchi

Frontiers in Cell and Developmental Biology, Vol

2021 Volume 9

Abstract	Cells internalize proteins and lipids in the plasma membrane (PM) and solutes in the extracellular space by endocytosis. The removal of PM by endocytosis is constantly balanced by the replenishment of proteins and lipids to PM through recycling pathway. Recycling endosomes (REs) are specific subsets of endosomes. Besides the established role of REs in recycling pathway, recent studies have revealed unanticipated roles of REs in membrane traffic and cell signalling. In this review, we highlight these emerging issues, with a particular focus on phosphatidylserine (PS), a phospholipid that is highly enriched in the cytosolic leaflet of RE membranes. We also discuss the pathogenesis of Hermansky Pudlak syndrome type 2 (HPS2) that arises from mutations in the AP3B1 gene, from the point of view of dysregulated RE functions.
Keywords	phosphatidylserine ; pleckstrin-homology domain ; flippase ; bioID proximity labeling ; endosomes ; membrane traffic ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-12-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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