Sorting of cargo in the tubular endosomal network

Solinger, Jachen A.; Spang, Anne

doi:10.1002/bies.202200158

Cited by 17 publications

(19 citation statements)

References 99 publications

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“…The membrane bound receptors are primarily recycled and return to the PM, but ligands are mostly delivered to the late endosome (LE) and then degraded. (French and Lauffenburger, 1997; Lakadamyali et al ., 2006; Solinger and Spang, 2022) We first examined if CLV3-TAMRA undergoes CME from the PM using AUXILIN-LIKE2 over-expression, which strongly hinders CME. (Adamowski et al ., 2018) After 60min of CLV3-TAMRA treatment, CLV3-TAMRA accumulated in the vacuole.…”

Section: Resultsmentioning

confidence: 99%

Macromolecular toolbox to elucidate CLE-RLK binding, signaling and downstream effects

Narasimhan,

Jahnke,

Kallert

et al. 2024

Preprint

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SummaryPlant peptides communicate by binding to a large family of receptor-like kinases (RLKs) and they share a conserved binding mechanism, which may account for their promiscuous interaction with several RLKs. In order to understand the in vivo binding specificity of CLE peptide family, we have developed a novel set of CLAVATA 3 (CLV3) based peptide tools. After carefully evaluating the CLE peptide binding characteristics, using solid phase synthesis process, we have modified the CLV3 peptide and attached a fluorophore and a photoactivable side group. We observed that the labeled CLV3 shows binding specificity within CLAVATA1 clade of RLKs while avoiding the distantly-related PEP RECEPTOR clade, thus resolving the contradictory results obtained previously by many in vitro methods. Furthermore, we observed that the RLK-bound CLV3 undergoes clathrin-mediated endocytosis and gets trafficked to vacuole via ARA7-labeled endosomes. Additionally, modifying CLV3 for light-controlled activation enabled spatial and temporal control over CLE signalling. Hence our CLV3 macromolecular toolbox can be used to study rapid cell specific down-stream effects. Given the conserved binding properties, in the future our toolbox can also be used as a template to modify other CLE peptides.HighlightA macromolecular tool box consisting of modified CLE peptide with fluorescent molecule and photoactivable group offers reliable insights into its in vivo binding characteristics, localization and signaling.

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Section: Resultsmentioning

confidence: 99%

Macromolecular toolbox to elucidate CLE-RLK binding, signaling and downstream effects

Narasimhan,

Jahnke,

Kallert

et al. 2024

Preprint

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“…5) tempts us to speculate that AP-3 could, in a similar manner, drive interaction and transfer of endocytosed proteins to endo-lysosomes. This would build on the emerging idea of a tubular endosomal network (TEN), which transiently exchanges cargoes with various endosomal compartments and transport carriers via kiss-and-run, thus mediating sorting of endo-lysosomal proteins 13 . AP-3 is reported to act in sorting from endosomes to melanosomes but its role in non-specialized cells is controversial 37 .…”

Section: Discussionmentioning

confidence: 99%

ARF1 compartments direct cargo flow via maturation into recycling endosomes

Stockhammer,

Adarska,

Natalia

et al. 2023

Preprint

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Cellular membrane homeostasis is maintained via a tightly regulated membrane and cargo flow between organelles of the endocytic and secretory pathways. Adaptor protein complexes (APs), which are recruited to membranes by the small GTPase ARF1, facilitate cargo selection and incorporation into trafficking intermediates. According to the classical model, small vesicles would facilitate bi-directional long-range vesicular transport between the Golgi and endosomes. Here we revisit the intracellular organization of the vesicular sorting machinery using a combination of CRISPR-Cas9 gene editing, live-cell high temporal (fast-confocal) or spatial (stimulated emission depletion (STED)) microscopy as well as correlative light and electron microscopy. We characterize novel tubulo-vesicular ARF1 compartments that harbor clathrin and different APs, and coordinate Golgi export as well as endocytic recycling. Rather than long-range vesicle shuttling, we observe transient interactions of ARF1 compartments and recycling endosomes, with the sorting machinery localizing at the interface between the two membranes. Our findings suggest that endocytic and secretory cargo transfer from ARF1 compartments to endosomes may be mediated by a kiss-and-run mechanism rather than by fusion of transport vesicles.

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“…Uptake mechanisms can be generally divided into clathrin-dependent and clathrin-independent endocytosis (CDE and CIE, respectively), after which internalized cargo is sorted within endosomes for delivery to distinct intracellular destinations (2). As membrane and fluid are added to the early endosome by incoming vesicles, narrow-diameter recycling tubules form, collecting a subset of cargo (3). Most plasma membrane lipids, and many types of internalized transmembrane proteins, are recycled back to the plasma membrane either directly (rapid recycling), indirectly via the endocytic recycling compartment (ERC) (slow recycling), or Golgi (retrograde recycling) (3, 4).…”

Section: Introductionmentioning

confidence: 99%

“…As membrane and fluid are added to the early endosome by incoming vesicles, narrow-diameter recycling tubules form, collecting a subset of cargo (3). Most plasma membrane lipids, and many types of internalized transmembrane proteins, are recycled back to the plasma membrane either directly (rapid recycling), indirectly via the endocytic recycling compartment (ERC) (slow recycling), or Golgi (retrograde recycling) (3, 4). As early endosomes mature they become late endosomes, eventually fusing with lysosomes, promoting degradation of remaining cargo.…”

Section: Introductionmentioning

confidence: 99%

“…As early endosomes mature they become late endosomes, eventually fusing with lysosomes, promoting degradation of remaining cargo. Many cellular processes depend upon accurate and efficient endocytic recycling, including cell migration, cell division, cell-cell fusion events, and control of neuronal signaling during learning and memory (3, 4). Trafficking pathways are often more elaborate in the context of polarized cells such as epithelia and neurons that maintain multiple functionally distinct plasma membrane domains, e.g.…”

Section: Introductionmentioning

confidence: 99%

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Syndapin Regulates the RAP-1 GTPase to Control Endocytic Recycling via RHO-1 and Non-Muscle Myosin II

Rodriguez-Polanco

Norris

Velasco

et al. 2023

Preprint

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After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F-BAR and SH3 domain Syndapin/PACSIN-family protein SDPN-1 is required in vivo for basolateral endocytic recycling in the C. elegans intestine. Here we sought to determine the significance of a predicted interaction between the SDPN-1 SH3 domain and a target sequence in PXF-1/PDZ-GEF1/RAPGEF2, a known exchange factor for Rap-GTPases. We found that endogenous mutations we engineered into the SDPN-1 SH3 domain, or its binding site in the PXF-1 protein, interfere with recycling in vivo, as does loss of the PXF-1 target RAP-1. Rap-GTPases have been shown in several contexts to negatively regulate RhoA activity. Our results show that RHO-1/RhoA is enriched on SDPN-1 and RAP-1 positive endosomes in the C. elegans intestine, and loss of SDPN-1 or RAP-1 elevates RHO-1(GTP) levels on intestinal endosomes. Furthermore, we found that depletion of RHO-1 suppressed sdpn-1 mutant recycling defects, indicating that control of RHO-1 activity is a key mechanism by which SDPN-1 acts to promote endocytic recycling. RHO-1/RhoA is well-known for controlling actomyosin contraction cycles, although little is known of non-muscle myosin II on endosomes. Our analysis found that non-muscle myosin II is enriched on SDPN-1 positive endosomes, with two non-muscle myosin II heavy chain isoforms acting in apparent opposition. Depletion of nmy-2 inhibited recycling like sdpn-1 mutants, while depletion of nmy-1 suppressed sdpn-1 mutant recycling defects, indicating actomyosin contractility in controlling recycling endosome function.

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Sorting of cargo in the tubular endosomal network

Cited by 17 publications

References 99 publications

Macromolecular toolbox to elucidate CLE-RLK binding, signaling and downstream effects

Macromolecular toolbox to elucidate CLE-RLK binding, signaling and downstream effects

ARF1 compartments direct cargo flow via maturation into recycling endosomes

Syndapin Regulates the RAP-1 GTPase to Control Endocytic Recycling via RHO-1 and Non-Muscle Myosin II

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