scholarly journals Peroxisomes, lipid droplets, and endoplasmic reticulum “hitchhike” on motile early endosomes

2015 ◽  
Vol 211 (5) ◽  
pp. 945-954 ◽  
Author(s):  
Sofia C. Guimaraes ◽  
Martin Schuster ◽  
Ewa Bielska ◽  
Gulay Dagdas ◽  
Sreedhar Kilaru ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Molecular Motors ◽  
Lipid Droplets ◽  
Intracellular Transport ◽  
Model System ◽  
Directed Transport ◽  
Intracellular Movement ◽  
Early Endosomes ◽  
Dependent Transport ◽  
First Time

Intracellular transport is mediated by molecular motors that bind cargo to be transported along the cytoskeleton. Here, we report, for the first time, that peroxisomes (POs), lipid droplets (LDs), and the endoplasmic reticulum (ER) rely on early endosomes (EEs) for intracellular movement in a fungal model system. We show that POs undergo kinesin-3– and dynein-dependent transport along microtubules. Surprisingly, kinesin-3 does not colocalize with POs. Instead, the motor moves EEs that drag the POs through the cell. PO motility is abolished when EE motility is blocked in various mutants. Most LD and ER motility also depends on EE motility, whereas mitochondria move independently of EEs. Covisualization studies show that EE-mediated ER motility is not required for PO or LD movement, suggesting that the organelles interact with EEs independently. In the absence of EE motility, POs and LDs cluster at the growing tip, whereas ER is partially retracted to subapical regions. Collectively, our results show that moving EEs interact transiently with other organelles, thereby mediating their directed transport and distribution in the cell.

scholarly journals Peroxisomes move by hitchhiking on early endosomes using the novel linker protein PxdA

2015 ◽  
Author(s):  
John Salogiannis ◽  
Martin J. Egan ◽  
Samara L. Reck-Peterson
Keyword(s):  
Molecular Motors ◽  
Intracellular Transport ◽  
Coiled Coil ◽  
Leading Edge ◽  
Time Lapse ◽  
Early Endosome ◽  
Organelle Transport ◽  
The Novel ◽  
Coiled Coil Region ◽  
Early Endosomes

Eukaryotic cells use microtubule-based intracellular transport for the delivery of many subcellular cargos, including organelles. The canonical view of organelle transport is that organelles directly recruit molecular motors via cargo-specific adaptors. In contrast to this view, we show here that peroxisomes move by hitchhiking on early endosomes, an organelle that directly recruits the transport machinery. Using the filamentous fungus Aspergillus nidulans we find that hitchhiking is mediated by a novel endosome-associated linker protein, PxdA. PxdA is required for normal distribution and long-range movement of peroxisomes, but not early endosomes or nuclei. Using simultaneous time-lapse imaging we find that early endosome-associated PxdA localizes to the leading edge of moving peroxisomes. We identify a coiled-coil region within PxdA that is necessary and sufficient for early endosome localization and peroxisome distribution and motility. These results present a new mechanism of microtubule-based organelle transport where peroxisomes hitchhike on early endosomes and identify PxdA as the novel linker protein required for this coupling.

scholarly journals Diffusion of kinesin motors on cargo can enhance binding and run lengths during intracellular transport

2019 ◽  
Author(s):  
Matthew Bovyn ◽  
Babu Reddy ◽  
Steven Gross ◽  
Jun Allard
Keyword(s):  
Computational Model ◽  
Molecular Motors ◽  
Lipid Droplets ◽  
Intracellular Transport ◽  
Control Point ◽  
Computational Studies ◽  
Organizational Changes ◽  
Surface Mobility ◽  
Viscosity Effects ◽  
Run Lengths

Cellular cargos, including lipid droplets and mitochondria, are transported along microtubules using molecular motors such as kinesins. Many experimental and computational studies of cargos with rigidly attached motors, in contrast to many biological cargos that have lipid surfaces that may allow surface mobility of motors. We extend a mechanochemical 3D computational model by adding coupled-viscosity effects to compare different motor arrangements and mobilities. We show that organizational changes can optimize for different objectives: Cargos with clustered motors are transported efficiently, but are slow to bind to microtubules, whereas those with motors dispersed rigidly on their surface bind microtubules quickly, but are transported inefficiently. Finally, cargos with freely-diffusing motors have both fast binding and efficient transport, although less efficient than clustered motors. These results suggest that experimentally observed changes in motor organization may be a control point for transport.

An Isolated Cytoskeletal Framework From Reticulomyxa: A New Model System For Intracellular Transport

1985 ◽  
Vol 43 ◽  
pp. 488-489
Author(s):  
Michael Koonce
Keyword(s):  
Intracellular Transport ◽  
Model System ◽  
Force Generation ◽  
Electron Microscopic ◽  
New Model ◽  
Directed Transport ◽  
Microscopic Studies ◽  
Intracellular Organelles

Pharmacological and correlative light and electron microscopic studies suggest that the two major cytoskeletal systems, the microtubules (MTs) and microfilaments (MFs), are involved in the directed transport of intracellular organelles. However, the details of organelle-cytoskeletal interactions and force generation are not known, nor is it clear whether transport is solely a MT or MF-based phenomenon, a coordinated effort, or if each system supports different classes of motility. Here I describe an isolated cytoskeletal “framework” derived from an unusual species of freshwater amoeba that provides a model system in which to examine these questions. We are intending to use this preparation to study the interactions with and movement of both isolated native and artificial organelles.

scholarly journals Novel contact sites between lipid droplets, early endosomes, and the endoplasmic reticulum

2020 ◽  
Vol 61 (11) ◽  
pp. 1364-1364
Author(s):  
Robert G. Parton ◽  
Marta Bosch ◽  
Bernhard Steiner ◽  
Albert Pol
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Contact Sites ◽  
Early Endosomes

scholarly journals The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis

2020 ◽  
Vol 133 (21) ◽  
pp. jcs248526 ◽  
Author(s):  
Wei Sheng Yap ◽  
Peter Shyu ◽  
Maria Laura Gaspar ◽  
Stephen A. Jesch ◽  
Charlie Marvalim ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Membrane Lipid ◽  
Model System ◽  
Lipid Homeostasis ◽  
Compensatory Mechanism ◽  
Unfolded Protein ◽  
Protein Response

ABSTRACTLipid droplets (LDs) are implicated in conditions of lipid and protein dysregulation. The fat storage-inducing transmembrane (FIT; also known as FITM) family induces LD formation. Here, we establish a model system to study the role of the Saccharomyces cerevisiae FIT homologues (ScFIT), SCS3 and YFT2, in the proteostasis and stress response pathways. While LD biogenesis and basal endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) remain unaltered in ScFIT mutants, SCS3 was found to be essential for proper stress-induced UPR activation and for viability in the absence of the sole yeast UPR transducer IRE1. Owing to not having a functional UPR, cells with mutated SCS3 exhibited an accumulation of triacylglycerol within the ER along with aberrant LD morphology, suggesting that there is a UPR-dependent compensatory mechanism that acts to mitigate lack of SCS3. Additionally, SCS3 was necessary to maintain phospholipid homeostasis. Strikingly, global protein ubiquitylation and the turnover of both ER and cytoplasmic misfolded proteins is impaired in ScFITΔ cells, while a screen for interacting partners of Scs3 identifies components of the proteostatic machinery as putative targets. Together, our data support a model where ScFITs play an important role in lipid metabolism and proteostasis beyond their defined roles in LD biogenesis.This article has an associated First Person interview with the first author of the paper.

scholarly journals Dynein Supports Motility of Endoplasmic Reticulum in the FungusUstilago maydis

2002 ◽  
Vol 13 (3) ◽  
pp. 965-977 ◽  
Author(s):  
Roland Wedlich-Söldner ◽  
Irene Schulz ◽  
Anne Straube ◽  
Gero Steinberg
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Intracellular Transport ◽  
Fluorescent Protein ◽  
Brefeldin A ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Minor Importance ◽  
Dependent Transport

The endoplasmic reticulum (ER) of most vertebrate cells is spread out by kinesin-dependent transport along microtubules, whereas studies in Saccharomyces cerevisiae indicated that motility of fungal ER is an actin-based process. However, microtubules are of minor importance for organelle transport in yeast, but they are crucial for intracellular transport within numerous other fungi. Herein, we set out to elucidate the role of the tubulin cytoskeleton in ER organization and dynamics in the fungal pathogen Ustilago maydis. An ER-resident green fluorescent protein (GFP)-fusion protein localized to a peripheral network and the nuclear envelope. Tubules and patches within the network exhibited rapid dynein-driven motion along microtubules, whereas conventional kinesin did not participate in ER motility. Cortical ER organization was independent of microtubules or F-actin, but reformation of the network after experimental disruption was mediated by microtubules and dynein. In addition, a polar gradient of motile ER-GFP stained dots was detected that accumulated around the apical Golgi apparatus. Both the gradient and the Golgi apparatus were sensitive to brefeldin A or benomyl treatment, suggesting that the gradient represents microtubule-dependent vesicle trafficking between ER and Golgi. Our results demonstrate a role of cytoplasmic dynein and microtubules in motility, but not peripheral localization of the ER inU. maydis.

scholarly journals PxdA interacts with the DipA phosphatase to regulate endosomal hitchhiking of peroxisomes

2021 ◽  
pp. mbc.E20-08-0559
Author(s):  
John Salogiannis ◽  
Jenna R. Christensen ◽  
Livia D. Songster ◽  
Adriana Aguilar-Maldonado ◽  
Nandini Shukla ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Molecular Mechanisms ◽  
Ustilago Maydis ◽  
Adaptor Proteins ◽  
Early Endosome ◽  
Alternative Mode ◽  
Ribonucleoprotein Complexes ◽  
Early Endosomes ◽  
Mode Of Transport

In canonical microtubule-based transport, adaptor proteins link cargos to dynein and kinesin motors. Recently, an alternative mode of transport known as ‘hitchhiking’ was discovered, where cargos achieve motility by hitching a ride on already-motile cargos, rather than attaching to a motor protein. Hitchhiking has been best-studied in two filamentous fungi, Aspergillus nidulans and Ustilago maydis. In U. maydis, ribonucleoprotein complexes, peroxisomes, lipid droplets, and endoplasmic reticulum hitchhike on early endosomes. In A. nidulans, peroxisomes hitchhike using a putative molecular linker, PxdA, which associates with early endosomes. However, whether other organelles use PxdA to hitchhike on early endosomes is unclear, as are the molecular mechanisms that regulate hitchhiking. Here we find that the proper distribution of lipid droplets, mitochondria and pre-autophagosomes do not require PxdA, suggesting that PxdA is a peroxisome-specific molecular linker. We identify two new pxdA alleles, including a point mutation (R2044P) that disrupts PxdA's ability to associate with early endosomes and reduces peroxisome movement. We also identify a novel regulator of peroxisome hitchhiking, the phosphatase DipA. DipA co-localizes with early endosomes and its early endosome-association relies on PxdA. Together, our data suggest that PxdA and the DipA phosphatase are specific regulators of peroxisome hitchhiking on early endosomes. [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text]

scholarly journals LIPID SYNTHESIS, INTRACELLULAR TRANSPORT, STORAGE, AND SECRETION

1967 ◽  
Vol 33 (2) ◽  
pp. 319-339 ◽  
Author(s):  
Olga Stein ◽  
Yechezkiel Stein
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Intracellular Transport ◽  
Lipid Synthesis ◽  
Water Soluble ◽  
Time Interval ◽  
Specimen Preparation ◽  
Electron Microscopic ◽  
Intracellular Movement ◽  
Lipid Product

A time sequence study of intracellular movement of labeled lipid in the liver was carried out on fasted and ethanol-treated rats injected with either palmitate-3H or glycerol-3H by electron microscopic radioautography. The elimination of water-soluble lipid precursors during specimen preparation was checked and found to be complete. The labeled lipid product in the tissue was identified as mostly triglyceride. A dehydration procedure was adapted to minimize the loss of lipid during specimen preparation. At 2 min after injection, the earliest time interval studied, both precursors were found to have penetrated the liver cells, and the label was found over both rough and smooth elements of the endoplasmic reticulum, which is the site of glyceride esterification. From 5 min on, in fasted and especially in ethanol-treated rats, the label was seen also over lipid droplets 0.5–2.0 µ in diameter, which represent "storage lipid" (slowly turning over compartment). Mitochondria became labeled mostly at later time intervals after injection. From 10 min on, concentration of label was seen over the Golgi apparatus, containing small osmiophilic particles. Association of label with groups of particles in smooth-surfaced vesicles and vacuoles in and near the Golgi apparatus and in the vicinity of the sinusoidal border was seen, both after palmitate-3H and glycerol-3H. It is proposed that these particles represent lipoproteins which are formed in the endoplasmic reticulum, "processed" in the Golgi apparatus, and transported in vacuoles to the sinusoid surface to be discharged into the circulation.

scholarly journals PxdA interacts with the DipA phosphatase to regulate endosomal hitchhiking of peroxisomes

2020 ◽  
Author(s):  
John Salogiannis ◽  
Jenna R. Christensen ◽  
Adriana Aguilar-Maldonado ◽  
Nandini Shukla ◽  
Samara L. Reck-Peterson
Keyword(s):  
Molecular Motors ◽  
Lipid Droplets ◽  
Molecular Mechanisms ◽  
Ustilago Maydis ◽  
Adaptor Proteins ◽  
Early Endosome ◽  
Alternative Mode ◽  
Ribonucleoprotein Complexes ◽  
Early Endosomes ◽  
Mode Of Transport

AbstractIn canonical microtubule-based transport, adaptor proteins link cargos to the molecular motors dynein and kinesin. Recently, an alternative mode of transport known as ‘hitchhiking’ was discovered, in which a cargo achieves motility by hitching a ride on an already-motile cargo, rather than attaching to a motor protein. Hitchhiking has been best-studied in two filamentous fungi, Aspergillus nidulans and Ustilago maydis. In U. maydis, ribonucleoprotein complexes, peroxisomes, lipid droplets, and endoplasmic reticulum all hitchhike on early endosomes. In A. nidulans, peroxisomes hitchhike using a putative molecular linker, PxdA, that associates with early endosomes. However, whether other organelles use PxdA to hitchhike on early endosomes is unclear, as are the molecular mechanisms that regulate hitchhiking in A. nidulans. Here we find that the proper distribution of lipid droplets, mitochondria and autophagosomes do not require PxdA, suggesting that PxdA is a molecular linker specific to peroxisomes. We also identify two new pxdA alleles, including a point mutation (R2044P) that disrupts PxdA’s ability to associate with early endosomes and reduces peroxisome movement. Finally, we identify a novel regulator of peroxisome hitchhiking, the phosphatase DipA. DipA co-localizes with early endosomes and its early endosome-association relies on PxdA.

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