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Article ; Online: Myoblast fusion: Experimental systems and cellular mechanisms.

Schejter, Eyal D

Seminars in cell & developmental biology

2016 Volume 60, Page(s) 112–120

Abstract: Fusion of myoblasts gives rise to the large, multi-nucleated muscle fibers that power and support organism motion and form. The mechanisms underlying this prominent form of cell-cell fusion have been investigated by a variety of experimental approaches, ... ...

Abstract	Fusion of myoblasts gives rise to the large, multi-nucleated muscle fibers that power and support organism motion and form. The mechanisms underlying this prominent form of cell-cell fusion have been investigated by a variety of experimental approaches, in several model systems. The purpose of this review is to describe and discuss recent progress in the field, as well as point out issues currently unresolved and worthy of further investigation. Following a description of several new experimental settings employed in the study of myoblast fusion, a series of topics relevant to the current understanding of the process are presented. These pertain to elements of three major cellular machineries- cell-adhesion, the actin-based cytoskeleton and membrane-associated elements- all of which play key roles in mediating myoblast fusion. Among the issues raised are the diversity of functions ascribed to different adhesion proteins (e.g. external cell apposition and internal recruitment of cytoskeleton regulators); functional significance of fusion-associated actin structures; and discussion of alternative mechanisms employing single or multiple fusion pore formation as the basis for muscle cell fusion.
Language	English
Publishing date	2016-12
Publishing country	England
Document type	Review ; Journal Article
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2016.07.016
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Article ; Online: Fusion pore dynamics of large secretory vesicles define a distinct mechanism of exocytosis.

Biton, Tom / Scher, Nadav / Carmon, Shari / Elbaz-Alon, Yael / Schejter, Eyal D / Shilo, Ben-Zion / Avinoam, Ori

The Journal of cell biology

2023 Volume 222, Issue 11

Abstract: Exocrine cells utilize large secretory vesicles (LSVs) up to 10 μm in diameter. LSVs fuse with the apical surface, often recruiting actomyosin to extrude their content through dynamic fusion pores. The molecular mechanism regulating pore dynamics remains ...

Abstract	Exocrine cells utilize large secretory vesicles (LSVs) up to 10 μm in diameter. LSVs fuse with the apical surface, often recruiting actomyosin to extrude their content through dynamic fusion pores. The molecular mechanism regulating pore dynamics remains largely uncharacterized. We observe that the fusion pores of LSVs in the Drosophila larval salivary glands expand, stabilize, and constrict. Arp2/3 is essential for pore expansion and stabilization, while myosin II is essential for pore constriction. We identify several Bin-Amphiphysin-Rvs (BAR) homology domain proteins that regulate fusion pore expansion and stabilization. We show that the I-BAR protein Missing-in-Metastasis (MIM) localizes to the fusion site and is essential for pore expansion and stabilization. The MIM I-BAR domain is essential but not sufficient for localization and function. We conclude that MIM acts in concert with actin, myosin II, and additional BAR-domain proteins to control fusion pore dynamics, mediating a distinct mode of exocytosis, which facilitates actomyosin-dependent content release that maintains apical membrane homeostasis during secretion.
MeSH term(s)	Animals ; Actin Cytoskeleton ; Actomyosin ; Cell Membrane ; Cytoskeletal Proteins ; Drosophila ; Exocytosis ; Secretory Vesicles/genetics
Chemical Substances	Actomyosin (9013-26-7) ; Cytoskeletal Proteins ; MIM protein, Drosophila
Language	English
Publishing date	2023-09-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202302112
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Article ; Online: Microtubules provide guidance cues for myofibril and sarcomere assembly and growth.

Dhanyasi, Nagaraju / VijayRaghavan, K / Shilo, Ben-Zion / Schejter, Eyal D

Developmental dynamics : an official publication of the American Association of Anatomists

2020 Volume 250, Issue 1, Page(s) 60–73

Abstract: Background: Muscle myofibrils and sarcomeres present exceptional examples of highly ordered cytoskeletal filament arrays, whose distinct spatial organization is an essential aspect of muscle cell functionality. We utilized ultra-structural analysis to ... ...

Abstract	Background: Muscle myofibrils and sarcomeres present exceptional examples of highly ordered cytoskeletal filament arrays, whose distinct spatial organization is an essential aspect of muscle cell functionality. We utilized ultra-structural analysis to investigate the assembly of myofibrils and sarcomeres within developing myotubes of the indirect flight musculature of Drosophila. Results: A temporal sequence composed of three major processes was identified: subdivision of the unorganized cytoplasm of nascent, multi-nucleated myotubes into distinct organelle-rich and filament-rich domains; initial organization of the filament-rich domains into myofibrils harboring nascent sarcomeric units; and finally, maturation of the highly-ordered pattern of sarcomeric thick (myosin-based) and thin (microfilament-based) filament arrays in parallel to myofibril radial growth. Significantly, organized microtubule arrays were present throughout these stages and exhibited dynamic changes in their spatial patterns consistent with instructive roles. Genetic manipulations confirm these notions, and imply specific and critical guidance activities of the microtubule-based cytoskeleton, as well as structural interdependence between the myosin- and actin-based filament arrays. Conclusions: Our observations highlight a surprisingly significant, behind-the-scenes role for microtubules in establishment of myofibril and sarcomere spatial patterns and size, and provide a detailed account of the interplay between major cytoskeletal elements in generating these essential contractile myogenic units.
MeSH term(s)	Animals ; Cytoskeleton/metabolism ; Drosophila/growth & development ; Drosophila/ultrastructure ; Muscle Development ; Pupa/ultrastructure ; Sarcomeres/metabolism
Language	English
Publishing date	2020-09-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1102541-4
ISSN	1097-0177 ; 1058-8388
ISSN (online)	1097-0177
ISSN	1058-8388
DOI	10.1002/dvdy.227
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Article ; Online: Generation and timing of graded responses to morphogen gradients.

Carmon, Shari / Jonas, Felix / Barkai, Naama / Schejter, Eyal D / Shilo, Ben-Zion

Development (Cambridge, England)

2021 Volume 148, Issue 24

Abstract: Morphogen gradients are known to subdivide a naive cell field into distinct zones of gene expression. Here, we examine whether morphogens can also induce a graded response within such domains. To this end, we explore the role of the Dorsal protein ... ...

Abstract	Morphogen gradients are known to subdivide a naive cell field into distinct zones of gene expression. Here, we examine whether morphogens can also induce a graded response within such domains. To this end, we explore the role of the Dorsal protein nuclear gradient along the dorsoventral axis in defining the graded pattern of actomyosin constriction that initiates gastrulation in early Drosophila embryos. Two complementary mechanisms for graded accumulation of mRNAs of crucial zygotic Dorsal target genes were identified. First, activation of target-gene expression expands over time from the ventral-most region of high nuclear Dorsal to lateral regions, where the levels are lower, as a result of a Dorsal-dependent activation probability of transcription sites. Thus, sites that are activated earlier will exhibit more mRNA accumulation. Second, once the sites are activated, the rate of RNA Polymerase II loading is also dependent on Dorsal levels. Morphological restrictions require that translation of the graded mRNA be delayed until completion of embryonic cell formation. Such timing is achieved by large introns, which provide a delay in production of the mature mRNAs. Spatio-temporal regulation of key zygotic genes therefore shapes the pattern of gastrulation.
MeSH term(s)	Animals ; Body Patterning/genetics ; Cell Nucleus/genetics ; Drosophila Proteins/genetics ; Drosophila melanogaster/genetics ; Embryo, Nonmammalian ; Embryonic Development/genetics ; Gastrulation/genetics ; Gene Expression Regulation, Developmental ; Introns/genetics ; Morphogenesis/genetics ; Nuclear Proteins/genetics ; Phosphoproteins/genetics ; RNA Polymerase II/genetics ; RNA, Messenger/genetics ; Transcription Factors/genetics
Chemical Substances	Drosophila Proteins ; Nuclear Proteins ; Phosphoproteins ; RNA, Messenger ; Transcription Factors ; dl protein, Drosophila ; RNA Polymerase II (EC 2.7.7.-)
Language	English
Publishing date	2021-12-17
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.199991
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Article ; Online: Exocytosis by vesicle crumpling maintains apical membrane homeostasis during exocrine secretion.

Kamalesh, Kumari / Scher, Nadav / Biton, Tom / Schejter, Eyal D / Shilo, Ben-Zion / Avinoam, Ori

Developmental cell

2021 Volume 56, Issue 11, Page(s) 1603–1616.e6

Abstract: Exocrine secretion commonly employs micron-scale vesicles that fuse to a limited apical surface, presenting an extreme challenge for maintaining membrane homeostasis. Using Drosophila melanogaster larval salivary glands, we show that the membranes of ... ...

Abstract	Exocrine secretion commonly employs micron-scale vesicles that fuse to a limited apical surface, presenting an extreme challenge for maintaining membrane homeostasis. Using Drosophila melanogaster larval salivary glands, we show that the membranes of fused vesicles undergo actomyosin-mediated folding and retention, which prevents them from incorporating into the apical surface. In addition, the diffusion of proteins and lipids between the fused vesicle and the apical surface is limited. Actomyosin contraction and membrane crumpling are essential for recruiting clathrin-mediated endocytosis to clear the retained vesicular membrane. Finally, we also observe membrane crumpling in secretory vesicles of the mouse exocrine pancreas. We conclude that membrane sequestration by crumpling followed by targeted endocytosis of the vesicular membrane, represents a general mechanism of exocytosis that maintains membrane homeostasis in exocrine tissues that employ large secretory vesicles.
MeSH term(s)	Actin Cytoskeleton/genetics ; Actomyosin/genetics ; Animals ; Biological Transport/genetics ; Cell Membrane/genetics ; Clathrin/genetics ; Drosophila melanogaster/genetics ; Endocytosis/genetics ; Exocrine Glands/metabolism ; Exocytosis/genetics ; Homeostasis/genetics ; Membrane Fusion/genetics ; Mice ; Salivary Glands/metabolism ; Salivary Glands/physiology ; Secretory Vesicles/genetics
Chemical Substances	Clathrin ; Actomyosin (9013-26-7)
Language	English
Publishing date	2021-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2021.05.004
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Zs.A 5742: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Delta traffic takes a sh-Arp turn.

Schejter, Eyal D

Nature cell biology

2009 Volume 11, Issue 7, Page(s) 791–793

Abstract: In the Notch pathway, the transmembrane ligand Delta is internalized and then re-established on the surface of signal-sending cells to allow the productive binding and activation of the Notch receptor on neighbouring cells. Arp2/3-dependent actin ... ...

Abstract	In the Notch pathway, the transmembrane ligand Delta is internalized and then re-established on the surface of signal-sending cells to allow the productive binding and activation of the Notch receptor on neighbouring cells. Arp2/3-dependent actin polymerization directs Delta trafficking through this circuit.
MeSH term(s)	Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Animals ; Drosophila Proteins/metabolism ; Drosophila Proteins/physiology ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Models, Biological ; Protein Binding/physiology ; Receptors, Notch/metabolism ; Receptors, Notch/physiology ; Signal Transduction/physiology
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Receptors, Notch ; delta protein
Language	English
Publishing date	2009-06-30
Publishing country	England
Document type	Comment ; News
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb0709-791
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Article ; Online: Feedback inhibition of actin on Rho mediates content release from large secretory vesicles.

Segal, Dagan / Zaritsky, Assaf / Schejter, Eyal D / Shilo, Ben-Zion

The Journal of cell biology

2018 Volume 217, Issue 5, Page(s) 1815–1826

Abstract: Secretion of adhesive glycoproteins to the lumen ... ...

Abstract	Secretion of adhesive glycoproteins to the lumen of
MeSH term(s)	Actins/metabolism ; Actomyosin/metabolism ; Amides/pharmacology ; Animals ; Depsipeptides/pharmacology ; Drosophila Proteins/metabolism ; Drosophila melanogaster/drug effects ; Drosophila melanogaster/metabolism ; Feedback, Physiological ; Gene Knockdown Techniques ; Models, Biological ; Profilins/metabolism ; Pyridines/pharmacology ; Secretory Vesicles/drug effects ; Secretory Vesicles/metabolism ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Actins ; Amides ; Depsipeptides ; Drosophila Proteins ; Profilins ; Pyridines ; chic protein, Drosophila ; jasplakinolide (102396-24-7) ; Y 27632 (138381-45-0) ; Actomyosin (9013-26-7) ; Rho1 protein, Drosophila (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2018-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201711006
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Article ; Online: Dynamics of Spaetzle morphogen shuttling in the

Rahimi, Neta / Averbukh, Inna / Carmon, Shari / Schejter, Eyal D / Barkai, Naama / Shilo, Ben-Zion

Development (Cambridge, England)

2019 Volume 146, Issue 21

Abstract: Establishment of morphogen gradients in the ... ...

Abstract	Establishment of morphogen gradients in the early
MeSH term(s)	Animals ; Body Patterning ; Cell Nucleus/physiology ; Drosophila/embryology ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Embryo, Nonmammalian/physiology ; Female ; Gastrula/metabolism ; Gastrulation ; Gene Expression Regulation, Developmental ; Intracellular Signaling Peptides and Proteins/genetics ; Male ; Morphogenesis ; Mutation ; Nuclear Proteins/physiology ; Phosphoproteins/physiology ; Signal Transduction ; Transcription Factors/physiology
Chemical Substances	Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins ; Phosphoproteins ; Transcription Factors ; WntD protein, Drosophila ; spz protein, Drosophila
Language	English
Publishing date	2019-11-12
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.181487
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Article ; Online: The

Shwartz, Arkadi / Dhanyasi, Nagaraju / Schejter, Eyal D / Shilo, Ben-Zion

eLife

2016 Volume 5

Abstract: Actin-based thin filament arrays constitute a fundamental core component of muscle sarcomeres. We have used formation of ... ...

Abstract	Actin-based thin filament arrays constitute a fundamental core component of muscle sarcomeres. We have used formation of the
Language	English
Publishing date	2016-10-12
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.16540
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Article ; Online: Orienting the direction of EGFR activation.

Shilo, Ben-Zion / Schejter, Eyal D

Developmental cell

2012 Volume 23, Issue 3, Page(s) 449–450

Abstract: Morphogens are typically distributed symmetrically from their source of production. In this issue of Developmental Cell, Peng et al. (2012) demonstrate that a bias in the directionality of protrusions emanating from cells secreting the EGFR ligand Spitz ... ...

Abstract	Morphogens are typically distributed symmetrically from their source of production. In this issue of Developmental Cell, Peng et al. (2012) demonstrate that a bias in the directionality of protrusions emanating from cells secreting the EGFR ligand Spitz leads to asymmetric activation of the pathway.
Language	English
Publishing date	2012-09-11
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2012.08.007
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