Mib1 contributes to persistent directional cell migration by regulating the Ctnnd1-Rac1 pathway

Mizoguchi, Takamasa; Ikeda, Shoko; Watanabe, Satoshi; Sugawara, Michiko; Itoh, Motoyuki

doi:10.1073/pnas.1712560114

Cited by 30 publications

(41 citation statements)

References 67 publications

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“…NICD injection allowed to restore midline crossing in mib1 ta52b mutants (Fig. 8e,f), establishing thereby that this morphogenetic defect is due to a loss of Notch signaling and not to additional, Notchindependent, functions of Mib1 in the regulation of cell migration 33 . Accordingly, midline crossing is also reduced in dld ; dla deficient embryos (Fig.…”

Section: Notch Signaling Governs Morphogenetic Cell Movements In the mentioning

confidence: 61%

“…In addition to its role in Delta ligand internalization, Mib1 also regulates the ubiquitination and endocytic trafficking of other substrate proteins 32,33 . This raises the question whether the neuroepithelial defects of Mib1-depleted embryos are due to the loss of Notch signaling or to a Notch-independent function of Mib1?…”

Section: Canonical Notch Signaling Is Required For the Morphogenesis mentioning

confidence: 99%

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Delta/Notch signaling controls neuroepithelial morphogenesis in the zebrafish spinal cord

Sharma

Saraswathy

et al. 2019

Preprint

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The morphogenesis of the nervous system requires coordinating the specification and differentiation of neural precursor cells, the establishment of neuroepithelial tissue architecture and the execution of specific cellular movements. How these aspects of neural development are linked is incompletely understood. Here we inactivate a major regulator of embryonic neurogenesis -the Delta/Notch pathway -and analyze the effect on zebrafish central nervous system morphogenesis. While some parts of the nervous system can establish neuroepithelial tissue architecture independently of Notch, Notch signaling is essential for spinal cord morphogenesis. In this tissue, Notch signaling is required to repress neuronal differentiation and promote neuroepithelial apico-basal polarity. Concomitant with a loss of their neuroepithelial properties, Notch signaling deficient cells also alter their morphogenetic behavior. In the wild-type zebrafish neural tube, cells divide at the organ midline to contribute one daughter cell to each organ half. Notch deficient animals fail to display this behavior and therefore form a misproportioned spinal cord. Taken together, our findings show that Notch signaling governs not only the cellular composition but also the morphogenetic shaping of the zebrafish spinal cord.

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Section: Notch Signaling Governs Morphogenetic Cell Movements In the mentioning

confidence: 61%

Section: Canonical Notch Signaling Is Required For the Morphogenesis mentioning

confidence: 99%

Delta/Notch signaling controls neuroepithelial morphogenesis in the zebrafish spinal cord

Sharma

Saraswathy

et al. 2019

Preprint

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“…3D). These include the inhibitor of the Arp2/3 complex, Arpin 50 , the breast cancer anti-estrogen resistance protein 3 (BCAR3) 51,52 , the PDZ and LIM domain protein 1 (PDLIM1/ELFIN) 53,54 , the SHC-transforming protein 1 (SHC1) 55 , the LIM and Calponin homology domain containing protein 1 (LIMCH1) 56 , the E3 ubiquitin ligase Mind Bomb 1 (MIB1) 57 , the microtubule-associated protein 4 (MAP4) 58 and the anthrax toxin and collagen I receptor, ANTXR1/ TEM8 59,60 . These observations strongly suggest that, through their control of actin organization, these proteins could be involved in invadosomes formation.…”

Section: Resultsmentioning

confidence: 99%

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

Thuault

Mamelonet

Salameh

et al. 2020

Sci Rep

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Supplementary Table S1: List of proteins biotinylated by Tks5-BirA* fusion protein. Protein list results from the comparison of proteins biotinylated by Tks5-BirA* fusion protein with proteins biotinylated by BirA* control protein, after their isolation by affinity capture and identification by mass spectrometry. Proteins listed here correspond to proteins above the full line indicative of protein hits obtained at a pFDR of 1% on Fig.3A volcano plot. For each protein their link to invadosome, their implication in actin cytoskeleton organization and their link to cancer invasion and metastasis have been analyzed, by comparison to the list of proteins obtained for "invadosome" query by GLAD4U literature mining and manual literature searching. The presence of Proline-rich regions and SH3 domains determined by InterPro site is also referenced. Data result from two different experiments processed three times. Supplementary Table S2: List of proteins biotinylated by PX-Tks5-BirA* fusion protein. Protein list results from the comparison of proteins biotinylated by PX-Tks5-BirA* fusion protein with proteins biotinylated by BirA* control protein, after their isolation by affinity capture and identification by mass spectrometry. Proteins listed here correspond to proteins hits obtained at a pFDR of 1%. Data result from two different experiments processed three times.

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“…Furthermore, as pointed out by the gene ontology analysis and manual literature searching, additional proteins involved in actin cytoskeleton organization were identified among Tks5 close neighbors ( Fig.3B -striped circles and Fig.3D). These include the inhibitor of the Arp2/3 complex, Arpin 49 , the breast cancer anti-estrogen resistance protein 3 (BCAR3) 50,51 , the PDZ and LIM domain protein 1 (PDLIM1/ELFIN) 52,53 , the SHC-transforming protein 1 (SHC1) 54 , the LIM and Calponin homology domain containing protein 1 (LIMCH1) 55 , the E3 ubiquitin ligase Mind Bomb 1 (MIB1) 56 , the microtubule-associated protein 4 (MAP4) 57 and the anthrax toxin and collagen I receptor, ANTXR1/TEM8 58,59 . These observations strongly suggest that, through their control of actin organization, these proteins could be involved in invadosomes formation.…”

Section: Tks5 Close Neighbors Belong To An Integrative Network Assocmentioning

confidence: 99%

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

Thuault

Mamelonet

Salameh

et al. 2019

Preprint

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ABSTRACTMetastatic progression is the leading cause of mortality in breast cancer. Invasive tumor cells develop invadopodia to travel through basement membranes and the interstitial matrix. Substantial efforts have been made to characterize invadopodia molecular composition. However, their full molecular identity is still missing due to the difficulty in isolating them. To fill this gap, we developed a non-hypothesis driven proteomic approach based on the BioID proximity biotinylation technology, using the invadopodia-specific protein Tks5α fused to the promiscuous biotin ligase BirA* as bait. In invasive breast cancer cells, Tks5α fusion concentrated to invadopodia and selectively biotinylated invadopodia components, in contrast to a fusion which lacked the membrane-targeting PX domain (Tks5β). Biotinylated proteins were isolated by affinity capture and identified by mass spectrometry. We identified known invadopodia components, revealing the pertinence of our strategy. Furthermore, we observed that Tks5 newly identified close neighbors belonged to a biologically relevant network centered on actin cytoskeleton organization. Analysis of Tks5β interactome demonstrated that some partners bound Tks5 before its recruitment to invadopodia. Thus, the present strategy allowed us to identify novel Tks5 partners that were not identified by traditional approaches and could help get a more comprehensive picture of invadopodia molecular landscape.

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Mib1 contributes to persistent directional cell migration by regulating the Ctnnd1-Rac1 pathway

Cited by 30 publications

References 67 publications

Delta/Notch signaling controls neuroepithelial morphogenesis in the zebrafish spinal cord

Delta/Notch signaling controls neuroepithelial morphogenesis in the zebrafish spinal cord

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

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