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Migrasomes provide regional cues for organ morphogenesis during zebrafish gastrulation

ABSTRACT: Migrasomes are recently identified vesicular organelles that form on retraction fibers behind migrating cells, cellular contents are released from migrasome by a process named migracytosis. The function of migrasomes in living organisms is unknown. Here we show that migrasomes are formed during zebrafish gastrulation, signaling molecules such as chemokines are enriched in migrasomes. Migrasomes are clustered on spatially restricted area in embryo where they provide regional cues for organ morphogenesis. Our study shown migrasome is signaling organelles which integrate spatial and specific biochemical information to coordinate migrating cells in complex biological processes such as morphogenesis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Danio Rerio (zebrafish) (brachydanio Rerio)

TISSUE(S): Embryo

SUBMITTER: Dong Jiang

LAB HEAD: Li Yu

PROVIDER: PXD013835 | Pride | 2019-06-03

REPOSITORIES: pride

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			Action	DRS
	MS181650-JD.pdResult	Other
	MS181650-JD1.raw	Raw
	MS181650-JD10.raw	Raw
	MS181650-JD11.raw	Raw
	MS181650-JD12.raw	Raw

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Migrasomes provide regional cues for organ morphogenesis during zebrafish gastrulation.

Jiang Dong D Jiang Zheng Z Lu Di D Wang Xuan X Liang Haisha H Zhang Junfeng J Meng Yaping Y Li Ying Y Wu Danni D Huang Yuwei Y Chen Yuling Y Deng Haiteng H Wu Qing Q Xiong Jingwei J Meng Anming A Yu Li L

Nature cell biology 20190801 8

Migrasomes are recently identified vesicular organelles that form on retraction fibres behind migrating cells. Whether migrasomes are present in vivo and, if so, the function of migrasomes in living organisms is unknown. Here, we show that migrasomes are formed during zebrafish gastrulation and signalling molecules, such as chemokines, are enriched in migrasomes. We further demonstrate that Tspan4 and Tspan7 are required for migrasome formation. Organ morphogenesis is impaired in zebrafish MZtsp ...[more]

PMID: 31371827

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Tetraspanin 4 stabilizes membrane swellings and facilitates their maturation into migrasomes

Project description:Migrasomes are newly discovered cell organelles forming by local swelling of retraction fibers. The migrasome formation critically depends on tetraspanin proteins present in the retraction fiber membranes and is modulated by the membrane tension and bending rigidity. It remained unknown how and in which time sequence these factors are involved in migrasome nucleation, growth, and stabilization, and what are the possible intermediate stages of migrasome biogenesis. Here using live cell imaging and biomimetic system for migrasomes and retraction fibers, we reveal that migrasome formation is a two-stage process. At the first stage, which in biomimetic system is mediated by membrane tension, local swellings largely devoid of tetraspanin 4 form on the retraction fibers. At the second stage, tetraspanin 4 molecules migrate toward and onto these swellings, which grow up to several microns in size and transform into migrasomes. This tetraspanin 4 recruitment to the swellings is essential for migrasome growth and stabilization. Based on these findings we propose that the major role of tetraspanin proteins is in stabilizing the migrasome structure while the migrasome nucleation and initial growth stages can be driven by membrane mechanical stresses.

2023-01-29 | PXD039664 | Pride

Rab10-CAV1 mediated intraluminal vesicles transport to migrasomes

Project description:Migrasomes, vesicular organelles generated on the retraction fibers of migrating cells, play a crucial role in migracytosis, mediating intercellular communication. The content cargoes determine the functional specificity of migrasomes. Migrasomes harbor numerous intraluminal vesicles, a pivotal component of their cargo. The mechanism underlying the transportation of these intraluminal vesicles to the migrasomes remain enigmatic. In this study, we identified a pathway by which Rab10-Caveolin1 mediates the transport of intraluminal vesicles to migrasomes. This intricate process necessitates the coordination of the motor protein Myosin Va, adaptor proteins RILPL2, facilitating vesicle transportation through retraction fibers to the migrasomes. Notably, the phosphorylation of Rab10 by the kinase LRRK2 augments this transport. Moreover, CSF-1 is selectively transported to migrasomes through this mechanism, subsequently fostering monocyte-macrophage differentiation in skin wound healing, which adds to our understanding of the physiological role of migrasomes.

2024-05-23 | PXD046146 |

Proteomic analysis of purified extracellular vesicles and crude migrasome from U87MG cells

Project description:This project has been performed to unveil the proteome of both purified extracellular vesicles (EVs) and crude migrasomes produced from U87MG gliolbastoma cells. Retraction fibers and migrasomes (R&Ms) are newly discovered membranous structures which are revealed to be generated by traction forces of migrating or deviding cells. However, it is still unknown what sorts of proteins are existed within these cellular structures. Thus, we performed the purification of both extracellular vesicles (EVs) and R&Ms (i.e., crude migrasome) from glioblastoma cells to validate the difference between EVs and R&Ms in terms of their protein components.

2024-01-14 | PXD047816 | Pride

Podocyte-released migrasomes in urine serve as an indicator for early podocyte injury

Project description:miRNA microarray was performed for migrasomes and exosomes derived from urine

2020-05-14 | GSE150459 | GEO

Lateral transfer of mRNA by migrasomes modifies the recipient cell

Project description:we report the discovery of migrasomal RNA. High-throughput deep sequencing was used to identifiy and quantify the RNAs in migrasome and cytosol

2020-05-06 | GSE130759 | GEO

Macrophage migrasomes (M-mig) gene profiling

Project description:In the present study, we have documented a previously unrecognized membrane vesicles called “migrasomes” (M-mig) that originate from the filament-like nanotubes of macrophage.To characterize the signatures of macrophage migrasomes (M-mig) gene expression that might underlie M-mig-associated biological function. M0-mig, M1-mig, M2-mig and HG-mig genome-wide expression profiling was carried out by using SurePrint G3 Mouse GE V2.0 8X60K Microarrays (Design ID:074809, Agilent Technologies, USA). Total RNA was quantified by the NanoDrop ND-2000 (Thermo Scientific) and the RNA integrity was assessed using Agilent Bioanalyzer 2100 (Agilent Technologies). The sample labeling, microarray hybridization and washing were performed based on the manufacturer’s standard protocols. Briefly, total RNA was transcribed to double strand cDNA, then synthesized into cRNA and labeled with Cyanine-3-CTP. The labeled cRNAs were hybridized onto the microarray. After washing, the arrays were scanned by the Agilent Scanner G2505C (Agilent Technologies). For data analysis, Feature Extraction software (version10.7.1.1, Agilent Technologies) was used to analyze array images to get raw data. Genespring (version14.9, Agilent Technologies) were employed to finish the basic analysis with the raw data. To begin with, the raw data was normalized with the quantile algorithm. Differentially expressed genes were then identified through fold change. The threshold set for up- and down-regulated genes was a fold change>=2.0. Afterwards, GO analysis and KEGG analysis were applied to determine the roles of these differentially expressed mRNAs.

2022-05-06 | E-MTAB-7994 | biostudies-arrayexpress

Identification of markers for migrasome detection

Project description:The migrasome is a newly discovered cellular organelle in migrating cells, first described in 20151,2. Migrasomes have been proposed to mediate cell-cell communications and may exert physiological and pathological effects. In zebrafish embryos, generation of migrasomes has been observed during gastrulation, and migrasomes have been shown to be essential for organ morphogenesis during embryonic development (Personal communication). Although migrasome-like structures have been detected by transmission electron microscopy (TEM) in various organs including eye, lung and intestine, definitive evidence for the presence of migrasomes in vivo in mammals is still lacking. Exosomes are defined as 30–100 nm extracellular vesicles derived from the multivesicular body and are secreted by a variety of cell types. Exosomes have attracted great attention in clinical studies since they were detected in solid tissues, such as cartilage3, and in biological fluids, such as blood4. One of the most commonly used methods for detection of extracellular vesicles (EVs) is a biochemical approach using known marker proteins. This strategy allows researchers to identify EVs in complex biological samples such as body fluids and tissues, and thus provides great flexibility for detection of EVs in vivo. So far, there is no satisfactory marker for biochemical detection of migrasomes. TSPAN4 and integrin are known to be enriched on migrasomes1,5. However, both proteins are also present on exosomes6, making it difficult to distinguish the two structures biochemically based only on detection of these proteins. Imaging is the only approach for confirming the presence of migrasomes, but it is not compatible with most clinical samples. Thus, there is an urgent need to identify migrasome-specific markers.

2021-06-28 | PXD026960 |

Neutrophil-derived migrasomes are an essential part of the coagulation system

Project description:Neutrophil-derived migrasomes are an essential part of the coagulation system, human

2024-05-07 | PXD051231 | Pride

Neutrophil-derived migrasomes are an essential part of the coagulation system

Project description:Neutrophil-derived migrasomes are an essential part of the coagulation system, mouse.

2024-05-07 | PXD051229 | Pride

Neutrophil-derived migrasomes are an essential part of the coagulation system

Project description:Neutrophil-derived migrasomes are an essential part of the coagulation system, Tspan9

2024-05-07 | PXD051246 | Pride