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Article ; Online: Synaptotagmin 7 docks synaptic vesicles to support facilitation and Doc2α-triggered asynchronous release.

Wu, Zhenyong / Kusick, Grant F / Berns, Manon M M / Raychaudhuri, Sumana / Itoh, Kie / Walter, Alexander M / Chapman, Edwin R / Watanabe, Shigeki

eLife

2024 Volume 12

Abstract: Despite decades of intense study, the molecular basis of asynchronous neurotransmitter release remains enigmatic. Synaptotagmin (syt) 7 and Doc2 have both been proposed as ... ...

Abstract	Despite decades of intense study, the molecular basis of asynchronous neurotransmitter release remains enigmatic. Synaptotagmin (syt) 7 and Doc2 have both been proposed as Ca
MeSH term(s)	Animals ; Mice ; Action Potentials ; Calcium/metabolism ; Exocytosis ; Neurotransmitter Agents ; Synapses/metabolism ; Synaptic Transmission ; Synaptic Vesicles/metabolism ; Synaptotagmin I/metabolism ; Synaptotagmins/metabolism ; Calcium-Binding Proteins/metabolism ; Nerve Tissue Proteins/metabolism
Chemical Substances	Calcium (SY7Q814VUP) ; Neurotransmitter Agents ; Synaptotagmin I ; Synaptotagmins (134193-27-4) ; Syt7 protein, mouse ; Doc2a protein, mouse ; Calcium-Binding Proteins ; Nerve Tissue Proteins
Language	English
Publishing date	2024-03-27
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.90632
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Molecular Basis of Mitochondrial and Peroxisomal Division Machineries.

Imoto, Yuuta / Itoh, Kie / Fujiki, Yukio

International journal of molecular sciences

2020 Volume 21, Issue 15

Abstract: Mitochondria and peroxisomes are ubiquitous subcellular organelles that are highly dynamic and possess a high degree of plasticity. These organelles proliferate through division of pre-existing organelles. Studies on yeast, mammalian cells, and ... ...

Abstract	Mitochondria and peroxisomes are ubiquitous subcellular organelles that are highly dynamic and possess a high degree of plasticity. These organelles proliferate through division of pre-existing organelles. Studies on yeast, mammalian cells, and unicellular algae have led to a surprising finding that mitochondria and peroxisomes share the components of their division machineries. At the heart of the mitochondrial and peroxisomal division machineries is a GTPase dynamin-like protein, Dnm1/Drp1, which forms a contractile ring around the neck of the dividing organelles. During division, Dnm1/Drp1 functions as a motor protein and constricts the membrane. This mechanochemical work is achieved by utilizing energy from GTP hydrolysis. Over the last two decades, studies have focused on the structure and assembly of Dnm1/Drp1 molecules around the neck. However, the regulation of GTP during the division of mitochondrion and peroxisome is not well understood. Here, we review the current understanding of Dnm1/Drp1-mediated divisions of mitochondria and peroxisomes, exploring the mechanisms of GTP regulation during the Dnm1/Drp1 function, and provide new perspectives on their potential contribution to mitochondrial and peroxisomal biogenesis.
MeSH term(s)	Animals ; Cell Division/genetics ; Dynamins/genetics ; GTP Phosphohydrolases/genetics ; Humans ; Mitochondria/genetics ; Mitochondrial Dynamics ; Mitochondrial Proteins/genetics ; Molecular Motor Proteins/genetics ; Peroxisomes/genetics ; Saccharomyces cerevisiae Proteins/genetics
Chemical Substances	Mitochondrial Proteins ; Molecular Motor Proteins ; Saccharomyces cerevisiae Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; DNM1 protein, S cerevisiae (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2020-07-30
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21155452
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Article ; Online: Defunctionalizing intracellular organelles such as mitochondria and peroxisomes with engineered phospholipase A/acyltransferases.

Watanabe, Satoshi / Nihongaki, Yuta / Itoh, Kie / Uyama, Toru / Toda, Satoshi / Watanabe, Shigeki / Inoue, Takanari

Nature communications

2022 Volume 13, Issue 1, Page(s) 4413

Abstract: Organelles vitally achieve multifaceted functions to maintain cellular homeostasis. Genetic and pharmacological approaches to manipulate individual organelles are powerful in probing their physiological roles. However, many of them are either slow in ... ...

Abstract	Organelles vitally achieve multifaceted functions to maintain cellular homeostasis. Genetic and pharmacological approaches to manipulate individual organelles are powerful in probing their physiological roles. However, many of them are either slow in action, limited to certain organelles, or rely on toxic agents. Here, we design a generalizable molecular tool utilizing phospholipase A/acyltransferases (PLAATs) for rapid defunctionalization of organelles via remodeling of the membrane phospholipids. In particular, we identify catalytically active PLAAT truncates with minimal unfavorable characteristics. Chemically-induced translocation of the optimized PLAAT to the mitochondria surface results in their rapid deformation in a phospholipase activity dependent manner, followed by loss of luminal proteins as well as dissipated membrane potential, thus invalidating the functionality. To demonstrate wide applicability, we then adapt the molecular tool in peroxisomes, and observe leakage of matrix-resident functional proteins. The technique is compatible with optogenetic control, viral delivery and operation in primary neuronal cultures. Due to such versatility, the PLAAT strategy should prove useful in studying organelle biology of diverse contexts.
MeSH term(s)	Acyltransferases/genetics ; Acyltransferases/metabolism ; Homeostasis ; Mitochondria/metabolism ; Organelles/metabolism ; Peroxisomes/metabolism ; Phospholipases/metabolism
Chemical Substances	Acyltransferases (EC 2.3.-) ; Phospholipases (EC 3.1.-)
Language	English
Publishing date	2022-07-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-31946-5
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Article: Dynamin 1xA interacts with Endophilin A1 via its spliced long C-terminus for ultrafast endocytosis.

Imoto, Yuuta / Xue, Jing / Luo, Lin / Raychaudhuri, Sumana / Itoh, Kie / Ma, Ye / Craft, George E / Kwan, Ann H / Mackay, Joel P / Ha, Taekjip / Watanabe, Shigeki / Robinson, Phillip J

bioRxiv : the preprint server for biology

2023

Abstract: Dynamin 1 (Dyn1) has two major splice variants, xA and xB, with unique C-terminal extensions of 20 and 7 amino acids, respectively. Of these, only Dyn1xA is enriched at endocytic zones and accelerates vesicle fission during ultrafast endocytosis. Here, ... ...

Abstract	Dynamin 1 (Dyn1) has two major splice variants, xA and xB, with unique C-terminal extensions of 20 and 7 amino acids, respectively. Of these, only Dyn1xA is enriched at endocytic zones and accelerates vesicle fission during ultrafast endocytosis. Here, we report that the long tail variant, Dyn1xA, achieves this localization by preferentially binding to Endophilin A through a newly defined Class II binding site overlapping with its extension, at a site spanning the splice boundary. Endophilin binds this site at higher affinity than the previously reported site, and this affinity is determined by amino acids outside the binding sites acting as long distance elements within the xA tail. Their interaction is regulated by the phosphorylation state of two serine residues specific to the xA variant. Dyn1xA and Endophilin colocalize in patches near the active zone of synapses. Mutations selectively disrupting Endophilin binding to the long extension cause Dyn1xA mislocalization along axons. In these mutants, endocytic pits are stalled on the plasma membrane during ultrafast endocytosis. These data suggest that the specificity for ultrafast endocytosis is defined by the phospho-regulated interaction of Endophilin A through a newly identified site of Dyn1xA's long tail.
Language	English
Publishing date	2023-09-24
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.09.21.558797
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Article ; Online: Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis.

Ogunmowo, Tyler H / Jing, Haoyuan / Raychaudhuri, Sumana / Kusick, Grant F / Imoto, Yuuta / Li, Shuo / Itoh, Kie / Ma, Ye / Jafri, Haani / Dalva, Matthew B / Chapman, Edwin R / Ha, Taekjip / Watanabe, Shigeki / Liu, Jian

Nature communications

2023 Volume 14, Issue 1, Page(s) 2888

Abstract: Compensatory endocytosis keeps the membrane surface area of secretory cells constant following exocytosis. At chemical synapses, clathrin-independent ultrafast endocytosis maintains such homeostasis. This endocytic pathway is temporally and spatially ... ...

Abstract	Compensatory endocytosis keeps the membrane surface area of secretory cells constant following exocytosis. At chemical synapses, clathrin-independent ultrafast endocytosis maintains such homeostasis. This endocytic pathway is temporally and spatially coupled to exocytosis; it initiates within 50 ms at the region immediately next to the active zone where vesicles fuse. However, the coupling mechanism is unknown. Here, we demonstrate that filamentous actin is organized as a ring, surrounding the active zone at mouse hippocampal synapses. Assuming the membrane area conservation is due to this actin ring, our theoretical model suggests that flattening of fused vesicles exerts lateral compression in the plasma membrane, resulting in rapid formation of endocytic pits at the border between the active zone and the surrounding actin-enriched region. Consistent with model predictions, our data show that ultrafast endocytosis requires sufficient compression by exocytosis of multiple vesicles and does not initiate when actin organization is disrupted, either pharmacologically or by ablation of the actin-binding protein Epsin1. Our work suggests that membrane mechanics underlie the rapid coupling of exocytosis to endocytosis at synapses.
MeSH term(s)	Animals ; Mice ; Synaptic Vesicles/metabolism ; Actins/metabolism ; Synapses/metabolism ; Endocytosis ; Cell Membrane/metabolism ; Exocytosis
Chemical Substances	Actins
Language	English
Publishing date	2023-05-20
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-38595-2
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Article: Assay to Measure Interactions between Purified Drp1 and Synthetic Liposomes.

Adachi, Yoshihiro / Itoh, Kie / Iijima, Miho / Sesaki, Hiromi

Bio-protocol

2017 Volume 7, Issue 9

Abstract: A mitochondrion is a dynamic intracellular organelle that actively divides and fuses to control its size, number and shape in cells. A regulated balance between mitochondrial division and fusion is fundamental to the function, distribution and turnover ... ...

Abstract	A mitochondrion is a dynamic intracellular organelle that actively divides and fuses to control its size, number and shape in cells. A regulated balance between mitochondrial division and fusion is fundamental to the function, distribution and turnover of mitochondria (Roy
Language	English
Publishing date	2017-08-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.2266
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Article ; Online: ActuAtor, a Listeria-inspired molecular tool for physical manipulation of intracellular organizations through de novo actin polymerization.

Nakamura, Hideki / Rho, Elmer / Lee, Christopher T / Itoh, Kie / Deng, Daqi / Watanabe, Satoshi / Razavi, Shiva / Matsubayashi, Hideaki T / Zhu, Cuncheng / Jung, Eleanor / Rangamani, Padmini / Watanabe, Shigeki / Inoue, Takanari

Cell reports

2023 Volume 42, Issue 10, Page(s) 113089

Abstract: Form and function are often interdependent throughout biology. Inside cells, mitochondria have particularly attracted attention since both their morphology and functionality are altered under pathophysiological conditions. However, directly assessing ... ...

Abstract	Form and function are often interdependent throughout biology. Inside cells, mitochondria have particularly attracted attention since both their morphology and functionality are altered under pathophysiological conditions. However, directly assessing their causal relationship has been beyond reach due to the limitations of manipulating mitochondrial morphology in a physiologically relevant manner. By engineering a bacterial actin regulator, ActA, we developed tools termed "ActuAtor" that inducibly trigger actin polymerization at arbitrary subcellular locations. The ActuAtor-mediated actin polymerization drives striking deformation and/or movement of target organelles, including mitochondria, Golgi apparatus, and nucleus. Notably, ActuAtor operation also disperses non-membrane-bound entities such as stress granules. We then implemented ActuAtor in functional assays, uncovering the physically fragmented mitochondria being slightly more susceptible to degradation, while none of the organelle functions tested are morphology dependent. The modular and genetically encoded features of ActuAtor should enable its application in studies of the form-function interplay in various intracellular contexts.
MeSH term(s)	Actins/metabolism ; Listeria/metabolism ; Listeria monocytogenes/physiology ; Polymerization ; Organelles/metabolism ; Bacterial Proteins/metabolism
Chemical Substances	Actins ; Bacterial Proteins
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.113089
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Article: Parkin suppresses Drp1-independent mitochondrial division

Roy, Madhuparna / Itoh, Kie / Iijima, Miho / Sesaki, Hiromi

Biochemical and biophysical research communications. 2016 July 01, v. 475

2016

Abstract: The cycle of mitochondrial division and fusion disconnect and reconnect individual mitochondria in cells to remodel this energy-producing organelle. Although dynamin-related protein 1 (Drp1) plays a major role in mitochondrial division in cells, a ... ...

Abstract	The cycle of mitochondrial division and fusion disconnect and reconnect individual mitochondria in cells to remodel this energy-producing organelle. Although dynamin-related protein 1 (Drp1) plays a major role in mitochondrial division in cells, a reduced level of mitochondrial division still persists even in the absence of Drp1. It is unknown how much Drp1-mediated mitochondrial division accounts for the connectivity of mitochondria. The role of a Parkinson’s disease-associated protein—parkin, which biochemically and genetically interacts with Drp1—in mitochondrial connectivity also remains poorly understood. Here, we quantified the number and connectivity of mitochondria using mitochondria-targeted photoactivatable GFP in cells. We show that the loss of Drp1 increases the connectivity of mitochondria by 15-fold in mouse embryonic fibroblasts (MEFs). While a single loss of parkin does not affect the connectivity of mitochondria, the connectivity of mitochondria significantly decreased compared with a single loss of Drp1 when parkin was lost in the absence of Drp1. Furthermore, the loss of parkin decreased the frequency of depolarization of the mitochondrial inner membrane that is caused by increased mitochondrial connectivity in Drp1-knockout MEFs. Therefore, our data suggest that parkin negatively regulates Drp1-indendent mitochondrial division.
Keywords	fibroblasts ; mice ; mitochondria ; mitochondrial membrane
Language	English
Dates of publication	2016-0701
Size	p. 283-288.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.05.038
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Article ; Online: Parkin suppresses Drp1-independent mitochondrial division.

Roy, Madhuparna / Itoh, Kie / Iijima, Miho / Sesaki, Hiromi

Biochemical and biophysical research communications

2016 Volume 475, Issue 3, Page(s) 283–288

Abstract	The cycle of mitochondrial division and fusion disconnect and reconnect individual mitochondria in cells to remodel this energy-producing organelle. Although dynamin-related protein 1 (Drp1) plays a major role in mitochondrial division in cells, a reduced level of mitochondrial division still persists even in the absence of Drp1. It is unknown how much Drp1-mediated mitochondrial division accounts for the connectivity of mitochondria. The role of a Parkinson's disease-associated protein-parkin, which biochemically and genetically interacts with Drp1-in mitochondrial connectivity also remains poorly understood. Here, we quantified the number and connectivity of mitochondria using mitochondria-targeted photoactivatable GFP in cells. We show that the loss of Drp1 increases the connectivity of mitochondria by 15-fold in mouse embryonic fibroblasts (MEFs). While a single loss of parkin does not affect the connectivity of mitochondria, the connectivity of mitochondria significantly decreased compared with a single loss of Drp1 when parkin was lost in the absence of Drp1. Furthermore, the loss of parkin decreased the frequency of depolarization of the mitochondrial inner membrane that is caused by increased mitochondrial connectivity in Drp1-knockout MEFs. Therefore, our data suggest that parkin negatively regulates Drp1-indendent mitochondrial division.
MeSH term(s)	Animals ; Calcium Signaling ; Cell Line ; Dynamins/metabolism ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Fibroblasts/ultrastructure ; Mice ; Microscopy, Fluorescence ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Turnover ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27) ; Dnm1l protein, mouse (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2016--01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.05.038
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Article ; Online: Maintenance of Cardiolipin and Crista Structure Requires Cooperative Functions of Mitochondrial Dynamics and Phospholipid Transport.

Kojima, Rieko / Kakimoto, Yuriko / Furuta, Shiina / Itoh, Kie / Sesaki, Hiromi / Endo, Toshiya / Tamura, Yasushi

Cell reports

2019 Volume 26, Issue 3, Page(s) 518–528.e6

Abstract: Mitochondria are dynamic organelles that constantly fuse and divide to maintain their proper morphology, which is essential for their normal functions. Energy production, a central role of mitochondria, demands highly folded structures of the ... ...

Abstract	Mitochondria are dynamic organelles that constantly fuse and divide to maintain their proper morphology, which is essential for their normal functions. Energy production, a central role of mitochondria, demands highly folded structures of the mitochondrial inner membrane (MIM) called cristae and a dimeric phospholipid (PL) cardiolipin (CL). Previous studies identified a number of factors involved in mitochondrial dynamics, crista formation, and CL biosynthesis, yet it is still enigmatic how these events are interconnected and cooperated. Here, we first report that mitochondrial fusion-division dynamics are important to maintain CL abundance. Second, our genetic and biochemical analyses revealed that intra-mitochondrial PL transport plays an important role in crista formation. Finally, we show that simultaneous defects in MIM fusion and intra-mitochondrial PL transport cause a drastic decrease in crista structure, resulting in CL depletion. These results expand our understanding of the integrated functional network among the PL transport, crista formation, and CL biogenesis.
MeSH term(s)	Cardiolipins/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Dynamics/genetics ; Phospholipids/metabolism
Chemical Substances	Cardiolipins ; Phospholipids
Language	English
Publishing date	2019-01-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.12.070
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