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Article ; Online: Myosin phosphatase targeting subunit1 controls localization and motility of Rab7-containing vesicles: Is myosin phosphatase a cytoplasmic dynein regulator?

Matsumura, Fumio / Murayama, Takashi / Kuriyama, Ryoko / Matsumura, Aya / Yamashiro, Shigeko

2024

Abstract: Myosin phosphatase targeting subunit1 (MYPT1) is a critical subunit of myosin phosphatase (MP), which brings PP1Cδ phosphatase and its substrate together. We previously showed that MYPT1 depletion resulted in oblique chromatid segregation. Therefore, we ... ...

Abstract	Myosin phosphatase targeting subunit1 (MYPT1) is a critical subunit of myosin phosphatase (MP), which brings PP1Cδ phosphatase and its substrate together. We previously showed that MYPT1 depletion resulted in oblique chromatid segregation. Therefore, we hypothesized that MYPT1 may control microtubule-dependent motor activity. Dynein, a minus-end microtubule motor, is known to be involved in mitotic spindle assembly. We thus examined whether MYPT1 and dynein may interact. Proximity ligation assay and co-immunoprecipitation revealed that MYPT1 and dynein intermediate chain (DIC) were associated. We found that DIC phosphorylation is increased in MYPT1-depleted cells in vivo, and that MP was able to dephosphorylate DIC in vitro. MYPT1 depletion also altered the localization and motility of Rab7-containing vesicles. MYPT1-depletion dispersed the perinuclear Rab7 localization to the peripheral in interphase cells. The dispersed Rab7 localization was rescued by microinjection of a constitutively active, truncated MYPT1 mutant, supporting that MP is responsible for the altered Rab7 localization. Analyses of Rab7 vesicle trafficking also revealed that minus-end transport was reduced in MYPT1-depleted cells. These results suggest an unexpected role of MP: MP controls dynein activity in both mitotic and interphase cells, possibly by dephosphorylating dynein subunits including DIC.
Language	English
Publishing date	2024-05-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	2534372-5
ISSN	1949-3592 ; 1949-3584
ISSN (online)	1949-3592
ISSN	1949-3584
DOI	10.1002/cm.21871
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Article: Functions of fascin in dendritic cells.

Yamashiro, Shigeko

Critical reviews in immunology

2012 Volume 32, Issue 1, Page(s) 11–21

Abstract: Fascin-1 is an actin-bundling protein that shares no homology with other actin-bundling proteins. It is greatly induced upon maturation of dendritic cells (DCs). However, fascin-1 is not expressed in other primary blood cells, including macrophages and ... ...

Abstract	Fascin-1 is an actin-bundling protein that shares no homology with other actin-bundling proteins. It is greatly induced upon maturation of dendritic cells (DCs). However, fascin-1 is not expressed in other primary blood cells, including macrophages and neutrophils, indicating a unique role of fascin-1 in the function of DCs upon maturation. An increasing body of evidence has shown that fascin-1 plays critical roles in maturation-associated DC functions, including dynamic assembly of veil-like membrane protrusions, disassembly of podosomes, migration to lymph nodes, and the assembly of the immunological synapse. Pathological analyses of fascin-1 expression revealed that fascin-1 is a useful marker of diseases of immune cells, including Langerhans cell histiocytosis and Hodgkin diseases. Furthermore, attempts have been made to explore the use of a fascin-1 promoter for DNA vaccination because it is strong and specific to DCs.
MeSH term(s)	Animals ; Biomarkers/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/immunology ; Carrier Proteins/metabolism ; Cell Differentiation ; Dendritic Cells/cytology ; Dendritic Cells/immunology ; Humans ; Microfilament Proteins/chemistry ; Microfilament Proteins/genetics ; Microfilament Proteins/immunology ; Microfilament Proteins/metabolism ; Promoter Regions, Genetic ; Vaccines, DNA/immunology
Chemical Substances	Biomarkers ; Carrier Proteins ; Microfilament Proteins ; Vaccines, DNA ; fascin (146808-54-0)
Language	English
Publishing date	2012-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1353116-5
ISSN	1040-8401
ISSN	1040-8401
DOI	10.1615/critrevimmunol.v32.i1.20
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Article ; Online: Investigation of Fascin1, a Marker of Mature Dendritic Cells, Reveals a New Role for IL-6 Signaling in CCR7-Mediated Chemotaxis.

Matsumura, Fumio / Polz, Robin / Singh, Sukhwinder / Matsumura, Aya / Scheller, Jürgen / Yamashiro, Shigeko

Journal of immunology (Baltimore, Md. : 1950)

2021 Volume 207, Issue 3, Page(s) 938–949

Abstract: Migration of mature dendritic cells (DCs) to lymph nodes is critical for the initiation of adaptive immunity. CCR7, a G-protein-coupled receptor for CCL19/21 chemokines, is known to be essential for chemotaxis of mature DCs, but the molecular mechanism ... ...

Abstract	Migration of mature dendritic cells (DCs) to lymph nodes is critical for the initiation of adaptive immunity. CCR7, a G-protein-coupled receptor for CCL19/21 chemokines, is known to be essential for chemotaxis of mature DCs, but the molecular mechanism linking inflammation to chemotaxis remains unclear. We previously demonstrated that fascin1, an actin-bundling protein, increases chemotaxis of mature mouse DCs. In this article, we demonstrated that fascin1 enhanced IL-6 secretion and signaling of mature mouse DCs. Furthermore, we demonstrated that IL-6 signaling is required for chemotaxis. Blockage of IL-6 signaling in wild-type DCs with an anti-IL-6 receptor α (IL-6Rα) Ab inhibited chemotaxis toward CCL19. Likewise, knockout of IL-6Rα inhibited chemotaxis of bone marrow-derived DCs. The addition of soluble IL-6Rα and IL-6 rescued chemotaxis of IL-6Rα knockout bone marrow-derived DCs, underscoring the role of IL-6 signaling in chemotaxis. We found that IL-6 signaling is required for internalization of CCR7, the initial step of CCR7 recycling. CCR7 recycling is essential for CCR7-mediated chemotaxis, explaining why IL-6 signaling is required for chemotaxis of mature DCs. Our results have identified IL-6 signaling as a new regulatory pathway for CCR7/CCL19-mediated chemotaxis and suggest that rapid migration of mature DCs to lymph nodes depends on inflammation-associated IL-6 signaling.
MeSH term(s)	Animals ; Antibodies, Blocking/pharmacology ; Antigens, Differentiation/genetics ; Antigens, Differentiation/metabolism ; Cell Differentiation ; Cells, Cultured ; Chemotaxis ; Dendritic Cells/immunology ; Gene Expression Regulation ; Interleukin-6/metabolism ; Mice ; Mice, Knockout ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Receptors, CCR7/metabolism ; Receptors, Interleukin-6/genetics ; Receptors, Interleukin-6/immunology ; Receptors, Interleukin-6/metabolism ; Receptors, Odorant/genetics ; Receptors, Odorant/metabolism ; Signal Transduction
Chemical Substances	Antibodies, Blocking ; Antigens, Differentiation ; Ccr7 protein, mouse ; Il6ra protein, mouse ; Interleukin-6 ; Microfilament Proteins ; Receptors, CCR7 ; Receptors, Interleukin-6 ; Receptors, Odorant ; fascin1 protein, mouse
Language	English
Publishing date	2021-07-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.2000318
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Article ; Online: Fascin confers resistance to Listeria infection in dendritic cells.

Matsumura, Fumio / Yamakita, Yoshihiko / Starovoytov, Val / Yamashiro, Shigeko

Journal of immunology (Baltimore, Md. : 1950)

2013 Volume 191, Issue 12, Page(s) 6156–6164

Abstract: Ag-presenting dendritic cells (DCs) must survive bacterial infection to present Ag information to naive T cells. The greater ability of DCs' host defense is evident from the report that DCs are more resistant to Listeria monocytogenes than macrophages. ... ...

Abstract	Ag-presenting dendritic cells (DCs) must survive bacterial infection to present Ag information to naive T cells. The greater ability of DCs' host defense is evident from the report that DCs are more resistant to Listeria monocytogenes than macrophages. However, the molecular mechanism of this resistance is unclear. We found that Listeria replicate more slowly in wild-type DCs compared with fascin1 knockout DCs. This finding is significant because fascin1, an actin-bundling protein, is specifically and greatly induced upon maturation of dendritic cells, but not other blood cells, including macrophages and neutrophils. Infection by Listeria makes phagosomes more acidic in wild-type DCs than in fascin1 knockout DCs, suggesting that fascin1 facilitates phagolysosomal fusion for killing of phagocytosed Listeria. We further found that fascin1 binds to LC3, an autophagosome marker, both in vivo and in vitro. Listeria are associated with LC3 to a greater extent in wild-type DCs than in fascin1 knockout DCs, suggesting that fascin1 facilitates autophagy for eradication of cytoplasmic Listeria. Taken together, our results suggest that fascin1 plays critical roles in the survival of DCs during Listeria infection, allowing DCs to function in innate and adaptive immunity.
MeSH term(s)	Animals ; Autophagy/physiology ; Dendritic Cells/immunology ; Dendritic Cells/microbiology ; Dendritic Cells/ultrastructure ; Immunity, Innate ; Listeria monocytogenes/growth & development ; Listeria monocytogenes/immunology ; Listeriosis/immunology ; Mice ; Mice, Knockout ; Microfilament Proteins/deficiency ; Microfilament Proteins/physiology ; Microscopy, Electron ; Microtubule-Associated Proteins/metabolism ; Phagosomes/chemistry ; Phagosomes/microbiology ; Phagosomes/physiology ; Protein Binding ; Receptors, Odorant ; Vacuoles/chemistry ; Vacuoles/physiology
Chemical Substances	Map1lc3b protein, mouse ; Microfilament Proteins ; Microtubule-Associated Proteins ; Receptors, Odorant ; fascin1 protein, mouse
Language	English
Publishing date	2013-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1300498
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Article ; Online: Myosin phosphatase-targeting subunit 1 controls chromatid segregation.

Matsumura, Fumio / Yamakita, Yoshihiko / Yamashiro, Shigeko

The Journal of biological chemistry

2011 Volume 286, Issue 12, Page(s) 10825–10833

Abstract: Myosin phosphatase is a heterotrimeric holoenzyme consisting of myosin phosphatase-targeting subunit 1 (MYPT1), a catalytic subunit of PP1Cβ, and a 20-kDa subunit of an unknown function. We have previously reported that myosin phosphatase also controls ... ...

Abstract	Myosin phosphatase is a heterotrimeric holoenzyme consisting of myosin phosphatase-targeting subunit 1 (MYPT1), a catalytic subunit of PP1Cβ, and a 20-kDa subunit of an unknown function. We have previously reported that myosin phosphatase also controls mitosis, apparently by antagonizing polo-like kinase 1 (PLK1). Here we found that depletion of MYPT1 by siRNA led to precocious chromatid segregation when HeLa cells were arrested at metaphase by a proteasome inhibitor, MG132, or by Cdc20 depletion. Consistently, cyclin B1 and securin were not degraded, indicating that the chromatid segregation is independent of the anaphase-promoting complex/cyclosome. Precocious segregation induced by MYPT1 depletion requires PLK1 activity because a PLK1 inhibitor, BI-2536, blocked precocious segregation. Furthermore, the expression of an unphosphorylatable mutant of SA2 (SCC3 homologue 2), a subunit of the cohesin complex, prevented precocious chromatid segregation induced by MYPT1 depletion. It has been shown that SA2 at centromeres is protected from phosphorylation by PP2A phosphatase recruited by Shugoshin (Sgo1), whereas SA2 along chromosome arms is phosphorylated by PLK1, leading to SA2 dissociation at chromosome arms. Taken together, our results suggest that hyperactivation of PLK1 caused by MYPT1 reduction could override the counteracting PP2A phosphatase, resulting in precocious chromatid segregation. We propose that SA2 at the centromeres is protected by two phosphatases. One is PP2A directly dephosphorylating SA2, and the other is myosin phosphatase counteracting PLK1.
MeSH term(s)	Cell Cycle Proteins/antagonists & inhibitors ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Centromere/genetics ; Centromere/metabolism ; Chromosome Segregation/drug effects ; Chromosome Segregation/physiology ; Chromosomes, Human/genetics ; Chromosomes, Human/metabolism ; HeLa Cells ; Humans ; Mutation ; Myosin-Light-Chain Phosphatase/genetics ; Myosin-Light-Chain Phosphatase/metabolism ; Phosphorylation/drug effects ; Phosphorylation/physiology ; Protein Phosphatase 2/genetics ; Protein Phosphatase 2/metabolism ; Protein Serine-Threonine Kinases/antagonists & inhibitors ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Pteridines/pharmacology ; Polo-Like Kinase 1
Chemical Substances	BI 2536 ; Cell Cycle Proteins ; Proto-Oncogene Proteins ; Pteridines ; SGO1 protein, human ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Protein Phosphatase 2 (EC 3.1.3.16) ; Myosin-Light-Chain Phosphatase (EC 3.1.3.53) ; PPP1R12A protein, human (EC 3.1.3.53)
Language	English
Publishing date	2011-01-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.169722
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Article ; Online: Myosin light chain kinases and phosphatase in mitosis and cytokinesis.

Matsumura, Fumio / Yamakita, Yoshihiko / Yamashiro, Shigeko

Archives of biochemistry and biophysics

2011 Volume 510, Issue 2, Page(s) 76–82

Abstract: At mitosis, cells undergo drastic alterations in morphology and cytoskeletal organization including cell rounding during prophase, mitotic spindle assembly during prometaphase and metaphase, chromatid segregation in anaphase, and cytokinesis during ... ...

Abstract	At mitosis, cells undergo drastic alterations in morphology and cytoskeletal organization including cell rounding during prophase, mitotic spindle assembly during prometaphase and metaphase, chromatid segregation in anaphase, and cytokinesis during telophase. It is well established that myosin II is a motor responsible for cytokinesis. Recent reports have indicated that myosin II is also involved in spindle assembly and karyokinesis. In this review, we summarize current understanding of the functions of myosin II in mitosis and cytokinesis of higher eukaryotes, and discuss the roles of possible upstream molecules that control myosin II in these mitotic events.
MeSH term(s)	Animals ; Cytokinesis ; Humans ; Mitosis ; Myosin Type II/metabolism ; Myosin-Light-Chain Kinase/metabolism ; Myosin-Light-Chain Phosphatase/metabolism
Chemical Substances	Myosin-Light-Chain Kinase (EC 2.7.11.18) ; Myosin-Light-Chain Phosphatase (EC 3.1.3.53) ; Myosin Type II (EC 3.6.1.-)
Language	English
Publishing date	2011-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2011.03.002
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Article ; Online: Fascin1 is dispensable for mouse development but is favorable for neonatal survival.

Yamakita, Yoshihiko / Matsumura, Fumio / Yamashiro, Shigeko

Cell motility and the cytoskeleton

2009 Volume 66, Issue 8, Page(s) 524–534

Abstract: Fascin1, an actin-bundling protein, has been demonstrated to be critical for filopodia formation in cultured cells, and thus is believed to be vital in motile activities including neurite extension and cell migration. To test whether fascin1 plays such ... ...

Abstract	Fascin1, an actin-bundling protein, has been demonstrated to be critical for filopodia formation in cultured cells, and thus is believed to be vital in motile activities including neurite extension and cell migration. To test whether fascin1 plays such essential roles within a whole animal, we have generated and characterized fascin1-deficient mice. Unexpectedly, fascin1-deficient mice are viable and fertile with no major developmental defect. Nissl staining of serial coronal brain sections reveals that fascin1-deficient brain is grossly normal except that knockout mouse brain lacks the posterior region of the anterior commissure neuron and has larger lateral ventricle. Fascin1-deficient, dorsal root ganglion neurons are able to extend neurites in vitro as well as those from wild-type mice, although fascin1-deficient growth cones are smaller and exhibit fewer and shorter filopodia than wild-type counterparts. Likewise, fascin1-deficient, embryonic fibroblasts are able to assemble filopodia, though filopodia are fewer, shorter and short-lived. These results indicate that fascin1-mediated filopodia assembly is dispensable for mouse development. Cell Motil. Cytoskeleton 2009. (c) 2009 Wiley-Liss, Inc.
MeSH term(s)	Animals ; Animals, Newborn ; Brain/cytology ; Brain/metabolism ; Cells, Cultured ; Embryonic Development/physiology ; Female ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Ganglia, Spinal/cytology ; Ganglia, Spinal/metabolism ; Male ; Mice ; Mice, Knockout ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Microscopy, Fluorescence ; Models, Genetic ; Neurons/cytology ; Neurons/metabolism ; Pseudopodia/metabolism ; Receptors, Odorant ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	Microfilament Proteins ; Receptors, Odorant ; fascin1 protein, mouse
Language	English
Publishing date	2009-04-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	283774-2
ISSN	1097-0169 ; 0886-1544
ISSN (online)	1097-0169
ISSN	0886-1544
DOI	10.1002/cm.20356
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Article: [Regulation of myosin II in cell division and cell migration].

Matsumura, Fumio / Yamakita, Yoshihiko / Yamashiro, Shigeko

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme

2006 Volume 51, Issue 6 Suppl, Page(s) 566–572

MeSH term(s)	Animals ; Cell Division/genetics ; Cell Movement/genetics ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Motor Proteins ; Myosin Type II/physiology ; Myosin-Light-Chain Kinase/physiology ; Phosphorylation ; Protein-Serine-Threonine Kinases/physiology ; Signal Transduction/genetics ; Signal Transduction/physiology ; Spindle Apparatus/genetics ; rho-Associated Kinases
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Molecular Motor Proteins ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; rho-Associated Kinases (EC 2.7.11.1) ; Myosin-Light-Chain Kinase (EC 2.7.11.18) ; Myosin Type II (EC 3.6.1.-)
Language	Japanese
Publishing date	2006-05
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	391163-9
ISSN	0039-9450
ISSN	0039-9450
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Article: Fascin 1 is dispensable for developmental and tumour angiogenesis.

Ma, Yafeng / Reynolds, Louise E / Li, Ang / Stevenson, Richard P / Hodivala-Dilke, Kairbaan M / Yamashiro, Shigeko / Machesky, Laura M

Biology open

2013 Volume 2, Issue 11, Page(s) 1187–1191

Abstract: The actin bundling protein fascin 1 is not expressed in adult epithelial tissues, but during development it is transiently expressed in many different cell types, and later in adults it is expressed in a subset of immune cells, nervous tissues, ... ...

Abstract	The actin bundling protein fascin 1 is not expressed in adult epithelial tissues, but during development it is transiently expressed in many different cell types, and later in adults it is expressed in a subset of immune cells, nervous tissues, endothelial cells, smooth muscle cells and pericytes. In contrast to the wealth of knowledge about the role of fascin 1 in cancer cell migration and invasion, little is known about the involvement of fascin 1 in angiogenesis. We speculated that as angiogenesis involves migration and invasion of tissues by endothelial cells, fascin 1 might have a role in both normal and tumour angiogenesis. Here, we provide evidence that loss of fascin 1 causes relatively minor reductions to angiogenesis during embryonic, postnatal and cancerous development by examining E12.5 hindbrains, postnatal retinas and B16F0 tumour cell allografts in fascin 1-null mice. We also find that in fascin 1 null tissues, endothelial cells display reduced filopodia formation during sprouting. We thus propose that fascin 1 expression promotes angiogenesis via filopodia formation, but is largely dispensable for both normal and tumour angiogenesis.
Language	English
Publishing date	2013-09-19
Publishing country	England
Document type	Journal Article
ZDB-ID	2632264-X
ISSN	2046-6390
ISSN	2046-6390
DOI	10.1242/bio.20136031
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Article ; Online: Fascin 1 is transiently expressed in mouse melanoblasts during development and promotes migration and proliferation.

Ma, Yafeng / Li, Ang / Faller, William J / Libertini, Silvana / Fiorito, Florencia / Gillespie, David A / Sansom, Owen J / Yamashiro, Shigeko / Machesky, Laura M

Development (Cambridge, England)

2013 Volume 140, Issue 10, Page(s) 2203–2211

Abstract: Fascins, a family of actin-bundling proteins, are expressed in a spatially and temporally restricted manner during development and often in cancer. Fascin 1 has a clear role in cell migration in vitro, but its role in vivo in mammals is not well ... ...

Abstract	Fascins, a family of actin-bundling proteins, are expressed in a spatially and temporally restricted manner during development and often in cancer. Fascin 1 has a clear role in cell migration in vitro, but its role in vivo in mammals is not well understood. Here, we investigate the role of fascin 1 in the melanocyte lineage and in melanoma cells. Fascin 1 knockout causes hypopigmentation in adult mice owing to migration and cell cycle progression defects in melanoblasts, the melanocyte precursor cell. Study of live embryo skin explants reveals that E14.5 fascin 1-null melanoblasts migrate slower, and generate fewer and thinner pseudopods. By contrast, fascin 1 expression drives faster migration and lamellipodia protrusion in melanocytes in vitro. In addition, fascin 1 depletion retards melanoblast proliferation in vivo and melanoma cell growth in vitro. These data indicate that fascin 1 not only promotes cell migration in mouse melanocytes but it also has a role in growth and cell cycle progression.
MeSH term(s)	Animals ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; Cell Cycle ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Gene Expression Regulation, Developmental ; Humans ; Melanocytes/cytology ; Melanoma/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Microfilament Proteins/genetics ; Microfilament Proteins/physiology ; Pigmentation ; Skin/pathology ; Time Factors
Chemical Substances	Carrier Proteins ; Microfilament Proteins ; fascin (146808-54-0)
Language	English
Publishing date	2013-04-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.089789
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