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Article ; Online: Erratum: Actin puts the squeeze on Drosophila glue secretion.

Merrifield, Christien J

2016 Volume 18, Issue 3, Page(s) 347

Language	English
Publishing date	2016-03
Publishing country	England
Document type	Published Erratum
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb3322
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Article ; Online: Actin puts the squeeze on Drosophila glue secretion.

Merrifield, Christien J

Nature cell biology

2016 Volume 18, Issue 2, Page(s) 142–144

Abstract: An actin filament coat promotes cargo expulsion from large exocytosing vesicles, but the mechanisms of coat formation and force generation have been poorly characterized. Elegant imaging studies of the Drosophila melanogaster salivary gland now reveal ... ...

Abstract	An actin filament coat promotes cargo expulsion from large exocytosing vesicles, but the mechanisms of coat formation and force generation have been poorly characterized. Elegant imaging studies of the Drosophila melanogaster salivary gland now reveal how actin and myosin are recruited, and show that myosin II forms a contractile 'cage' that facilitates exocytosis.
MeSH term(s)	Actomyosin/metabolism ; Animals ; Carrier Proteins/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Exocytosis ; Glue Proteins, Drosophila/metabolism ; Membrane Proteins/metabolism ; Salivary Glands/metabolism ; Secretory Vesicles/metabolism
Chemical Substances	Carrier Proteins ; Drosophila Proteins ; Glue Proteins, Drosophila ; Membrane Proteins ; Actomyosin (9013-26-7)
Language	English
Publishing date	2016-02
Publishing country	England
Document type	Comment ; Journal Article
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb3305
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Zs.A 5169: 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: Fishing for clathrin-coated pit nucleators.

Merrifield, Christien J

Nature cell biology

2012 Volume 14, Issue 5, Page(s) 452–454

Abstract: The membrane-curvature-inducing protein Fcho was proposed to be part of a ubiquitous nucleation mechanism for clathrin-coated pits. However, studies in developing zebrafish embryos now indicate a role for Fcho as a receptor-specific adaptor in bone ... ...

Abstract	The membrane-curvature-inducing protein Fcho was proposed to be part of a ubiquitous nucleation mechanism for clathrin-coated pits. However, studies in developing zebrafish embryos now indicate a role for Fcho as a receptor-specific adaptor in bone morphogenetic protein (BMP) signalling, rather than a global coated-pit nucleator.
MeSH term(s)	Adaptor Protein Complex 2/physiology ; Body Patterning ; Clathrin/metabolism ; Endocytosis ; Fatty Acid-Binding Proteins ; Humans ; Membrane Proteins ; Proteins/physiology
Chemical Substances	Adaptor Protein Complex 2 ; Clathrin ; FCHO1 protein, human ; FCHO2 protein, human ; Fatty Acid-Binding Proteins ; Membrane Proteins ; Proteins
Language	English
Publishing date	2012-05-02
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb2497
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Article ; Online: Single molecule super-resolution imaging of bacterial cell pole proteins with high-throughput quantitative analysis pipeline.

Altinoglu, Ipek / Merrifield, Christien J / Yamaichi, Yoshiharu

Scientific reports

2019 Volume 9, Issue 1, Page(s) 6680

Abstract: Bacteria show sophisticated control of their cellular organization, and many bacteria deploy different polar landmark proteins to organize the cell pole. Super-resolution microscopy, such as Photo-Activated Localization Microscopy (PALM), provides the ... ...

Abstract	Bacteria show sophisticated control of their cellular organization, and many bacteria deploy different polar landmark proteins to organize the cell pole. Super-resolution microscopy, such as Photo-Activated Localization Microscopy (PALM), provides the nanoscale localization of molecules and is crucial for better understanding of organization and dynamics in single-molecule. However, analytical tools are not fully available yet, in particular for bacterial cell biology. For example, quantitative and statistical analyses of subcellular localization with multiple cells from multiple fields of view are lacking. Furthermore, brightfield images are not sufficient to get accurate contours of small and low contrast bacterial cells, compared to subpixel presentation of target molecules. Here we describe a novel analytic tool for PALM which integrates precisely drawn cell outlines, of either inner membrane or periplasm, labelled by PALM-compatible fluorescent protein fusions, with molecule data for >10,000 molecules from >100 cells by fitting each cell into an oval arc. In the vibrioid bacterium Vibrio cholerae, the polar anchor HubP constitutes a big polar complex which includes multiple proteins involved in chemotaxis and the flagellum. With this pipeline, HubP is shown to be slightly skewed towards the inner curvature side of the cell, while its interaction partners showed rather loose polar localization.
MeSH term(s)	Bacteria/metabolism ; Bacterial Proteins/metabolism ; Fluorescent Antibody Technique ; Gene Expression Regulation, Bacterial ; Molecular Imaging/methods ; Single Molecule Imaging/methods
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2019-04-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-43051-7
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Article ; Online: Single molecule super-resolution imaging of bacterial cell pole proteins with high-throughput quantitative analysis pipeline

Ipek Altinoglu / Christien J. Merrifield / Yoshiharu Yamaichi

Scientific Reports, Vol 9, Iss 1, Pp 1-

2019 Volume 11

Abstract: Abstract Bacteria show sophisticated control of their cellular organization, and many bacteria deploy different polar landmark proteins to organize the cell pole. Super-resolution microscopy, such as Photo-Activated Localization Microscopy (PALM), ... ...

Abstract	Abstract Bacteria show sophisticated control of their cellular organization, and many bacteria deploy different polar landmark proteins to organize the cell pole. Super-resolution microscopy, such as Photo-Activated Localization Microscopy (PALM), provides the nanoscale localization of molecules and is crucial for better understanding of organization and dynamics in single-molecule. However, analytical tools are not fully available yet, in particular for bacterial cell biology. For example, quantitative and statistical analyses of subcellular localization with multiple cells from multiple fields of view are lacking. Furthermore, brightfield images are not sufficient to get accurate contours of small and low contrast bacterial cells, compared to subpixel presentation of target molecules. Here we describe a novel analytic tool for PALM which integrates precisely drawn cell outlines, of either inner membrane or periplasm, labelled by PALM-compatible fluorescent protein fusions, with molecule data for >10,000 molecules from >100 cells by fitting each cell into an oval arc. In the vibrioid bacterium Vibrio cholerae, the polar anchor HubP constitutes a big polar complex which includes multiple proteins involved in chemotaxis and the flagellum. With this pipeline, HubP is shown to be slightly skewed towards the inner curvature side of the cell, while its interaction partners showed rather loose polar localization.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2019-04-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Endocytic accessory factors and regulation of clathrin-mediated endocytosis.

Merrifield, Christien J / Kaksonen, Marko

Cold Spring Harbor perspectives in biology

2014 Volume 6, Issue 11, Page(s) a016733

Abstract: Up to 60 different proteins are recruited to the site of clathrin-mediated endocytosis in an ordered sequence. These accessory proteins have roles during all the different stages of clathrin-mediated endocytosis. First, they participate in the initiation ...

Abstract	Up to 60 different proteins are recruited to the site of clathrin-mediated endocytosis in an ordered sequence. These accessory proteins have roles during all the different stages of clathrin-mediated endocytosis. First, they participate in the initiation of the endocytic event, thereby determining when and where endocytic vesicles are made; later they are involved in the maturation of the clathrin coat, recruitment of specific cargo molecules, bending of the membrane, and finally in scission and uncoating of the nascent vesicle. In addition, many of the accessory components are involved in regulating and coupling the actin cytoskeleton to the endocytic membrane. We will discuss the different accessory components and their various roles. Most of the data comes from studies performed with cultured mammalian cells or yeast cells. The process of endocytosis is well conserved between these different organisms, but there are also many interesting differences that may shed light on the mechanistic principles of endocytosis.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Clathrin-Coated Vesicles/metabolism ; Clathrin-Coated Vesicles/physiology ; Endocytosis/physiology ; Mammals/metabolism ; Models, Biological ; Yeasts/cytology ; Yeasts/metabolism
Language	English
Publishing date	2014-10-03
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a016733
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Article: Seeing is believing: imaging actin dynamics at single sites of endocytosis.

Merrifield, Christien J

Trends in cell biology

2004 Volume 14, Issue 7, Page(s) 352–358

Abstract: Endocytosis is characterized by movement and precisely controlled changes in membrane geometry during vesicle formation. Recent developments in live-cell imaging have enabled such movements to be monitored in vivo and correlated with the recruitment and ... ...

Abstract	Endocytosis is characterized by movement and precisely controlled changes in membrane geometry during vesicle formation. Recent developments in live-cell imaging have enabled such movements to be monitored in vivo and correlated with the recruitment and dismissal of fluorescently labeled proteins. This experimental strategy has revealed the sequential recruitment of proteins that are involved in actin polymerization, and actin to single sites of endocytosis in both yeast and mammalian cells. Actin polymerization is correlated with the inward movements of endocytic organelles, which suggests that actin polymerization has a conserved role in this process. In this article, I will discuss three models for the role of actin polymerization in endocytosis.
MeSH term(s)	Actins/physiology ; Animals ; Clathrin/chemistry ; Endocytosis/physiology ; Fibroblasts/physiology ; Models, Biological ; Organelles/physiology ; Yeasts/physiology
Chemical Substances	Actins ; Clathrin
Language	English
Publishing date	2004-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2004.05.008
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Article ; Online: A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis.

Taylor, Marcus J / Lampe, Marko / Merrifield, Christien J

PLoS biology

2012 Volume 10, Issue 4, Page(s) e1001302

Abstract: Clathrin-mediated endocytosis proceeds by a sequential series of reactions catalyzed by discrete sets of protein machinery. The final reaction in clathrin-mediated endocytosis is membrane scission, which is mediated by the large guanosine triophosphate ... ...

Abstract	Clathrin-mediated endocytosis proceeds by a sequential series of reactions catalyzed by discrete sets of protein machinery. The final reaction in clathrin-mediated endocytosis is membrane scission, which is mediated by the large guanosine triophosphate hydrolase (GTPase) dynamin and which may involve the actin-dependent recruitment of N-terminal containing BIN/Amphiphysin/RVS domain containing (N-BAR) proteins. Optical microscopy has revealed a detailed picture of when and where particular protein types are recruited in the ∼20-30 s preceding scission. Nevertheless, the regulatory mechanisms and functions that underpin protein recruitment are not well understood. Here we used an optical assay to investigate the coordination and interdependencies between the recruitment of dynamin, the actin cytoskeleton, and N-BAR proteins to individual clathrin-mediated endocytic scission events. These measurements revealed that a feedback loop exists between dynamin and actin at sites of membrane scission. The kinetics of dynamin, actin, and N-BAR protein recruitment were modulated by dynamin GTPase activity. Conversely, acute ablation of actin dynamics using latrunculin-B led to a ∼50% decrease in the incidence of scission, an ∼50% decrease in the amplitude of dynamin recruitment, and abolished actin and N-BAR recruitment to scission events. Collectively these data suggest that dynamin, actin, and N-BAR proteins work cooperatively to efficiently catalyze membrane scission. Dynamin controls its own recruitment to scission events by modulating the kinetics of actin and N-BAR recruitment to sites of scission. Conversely actin serves as a dynamic scaffold that concentrates dynamin and N-BAR proteins at sites of scission.
MeSH term(s)	Actins/antagonists & inhibitors ; Actins/metabolism ; Animals ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Cell Membrane/metabolism ; Clathrin/metabolism ; Clathrin-Coated Vesicles/metabolism ; Clathrin-Coated Vesicles/ultrastructure ; Cytoskeletal Proteins/metabolism ; Dynamin I/genetics ; Dynamin I/metabolism ; Endocytosis ; Feedback, Physiological ; Kinetics ; Mice ; Mutation, Missense ; NIH 3T3 Cells ; Protein Serine-Threonine Kinases/metabolism ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Thiazolidines/pharmacology
Chemical Substances	Actins ; Bridged Bicyclo Compounds, Heterocyclic ; Clathrin ; Cytoskeletal Proteins ; Recombinant Fusion Proteins ; Thiazolidines ; GAK protein, mouse (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Dynamin I (EC 3.5.1.50) ; latrunculin B (LW7U308U7U)
Language	English
Publishing date	2012-04-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.1001302
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Article ; Online: A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis.

Marcus J Taylor / Marko Lampe / Christien J Merrifield

PLoS Biology, Vol 10, Iss 4, p e

2012 Volume 1001302

Abstract	Clathrin-mediated endocytosis proceeds by a sequential series of reactions catalyzed by discrete sets of protein machinery. The final reaction in clathrin-mediated endocytosis is membrane scission, which is mediated by the large guanosine triophosphate hydrolase (GTPase) dynamin and which may involve the actin-dependent recruitment of N-terminal containing BIN/Amphiphysin/RVS domain containing (N-BAR) proteins. Optical microscopy has revealed a detailed picture of when and where particular protein types are recruited in the ∼20-30 s preceding scission. Nevertheless, the regulatory mechanisms and functions that underpin protein recruitment are not well understood. Here we used an optical assay to investigate the coordination and interdependencies between the recruitment of dynamin, the actin cytoskeleton, and N-BAR proteins to individual clathrin-mediated endocytic scission events. These measurements revealed that a feedback loop exists between dynamin and actin at sites of membrane scission. The kinetics of dynamin, actin, and N-BAR protein recruitment were modulated by dynamin GTPase activity. Conversely, acute ablation of actin dynamics using latrunculin-B led to a ∼50% decrease in the incidence of scission, an ∼50% decrease in the amplitude of dynamin recruitment, and abolished actin and N-BAR recruitment to scission events. Collectively these data suggest that dynamin, actin, and N-BAR proteins work cooperatively to efficiently catalyze membrane scission. Dynamin controls its own recruitment to scission events by modulating the kinetics of actin and N-BAR recruitment to sites of scission. Conversely actin serves as a dynamic scaffold that concentrates dynamin and N-BAR proteins at sites of scission.
Keywords	Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis.

Taylor, Marcus J / Perrais, David / Merrifield, Christien J

PLoS biology

2011 Volume 9, Issue 3, Page(s) e1000604

Abstract: Dual colour total internal reflection fluorescence microscopy is a powerful tool for decoding the molecular dynamics of clathrin-mediated endocytosis (CME). Typically, the recruitment of a fluorescent protein-tagged endocytic protein was referenced to ... ...

Abstract	Dual colour total internal reflection fluorescence microscopy is a powerful tool for decoding the molecular dynamics of clathrin-mediated endocytosis (CME). Typically, the recruitment of a fluorescent protein-tagged endocytic protein was referenced to the disappearance of spot-like clathrin-coated structure (CCS), but the precision of spot-like CCS disappearance as a marker for canonical CME remained unknown. Here we have used an imaging assay based on total internal reflection fluorescence microscopy to detect scission events with a resolution of ∼ 2 s. We found that scission events engulfed comparable amounts of transferrin receptor cargo at CCSs of different sizes and CCS did not always disappear following scission. We measured the recruitment dynamics of 34 types of endocytic protein to scission events: Abp1, ACK1, amphiphysin1, APPL1, Arp3, BIN1, CALM, CIP4, clathrin light chain (Clc), cofilin, coronin1B, cortactin, dynamin1/2, endophilin2, Eps15, Eps8, epsin2, FBP17, FCHo1/2, GAK, Hip1R, lifeAct, mu2 subunit of the AP2 complex, myosin1E, myosin6, NECAP, N-WASP, OCRL1, Rab5, SNX9, synaptojanin2β1, and syndapin2. For each protein we aligned ∼ 1,000 recruitment profiles to their respective scission events and constructed characteristic "recruitment signatures" that were grouped, as for yeast, to reveal the modular organization of mammalian CME. A detailed analysis revealed the unanticipated recruitment dynamics of SNX9, FBP17, and CIP4 and showed that the same set of proteins was recruited, in the same order, to scission events at CCSs of different sizes and lifetimes. Collectively these data reveal the fine-grained temporal structure of CME and suggest a simplified canonical model of mammalian CME in which the same core mechanism of CME, involving actin, operates at CCSs of diverse sizes and lifetimes.
MeSH term(s)	Actins/metabolism ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; Dynamins/metabolism ; Endocytosis ; Mammals/metabolism ; Mice ; Molecular Dynamics Simulation ; Myosins/metabolism ; NIH 3T3 Cells ; Polymerization ; Protein Binding ; Protein Structure, Tertiary ; Time Factors
Chemical Substances	Actins ; Adaptor Proteins, Signal Transducing ; Clathrin ; Myosins (EC 3.6.4.1) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2011-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.1000604
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