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Article ; Online: Special issue on "Cell stress in development, aging and disease".

van Oosten-Hawle, Patricija / Saarikangas, Juha

2021 Volume 408, Issue 1, Page(s) 112839

MeSH term(s)	Aging ; Animals ; Humans ; Research ; Stress, Physiological/physiology
Language	English
Publishing date	2021-09-21
Publishing country	United States
Document type	Editorial ; Introductory Journal Article
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2021.112839
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Article: Proteostatic tuning underpins the evolution of novel multicellular traits.

Montrose, Kristopher / Lac, Dung T / Burnetti, Anthony J / Tong, Kai / Ozan Bozdag, G / Hukkanen, Mikaela / Ratcliff, William C / Saarikangas, Juha

bioRxiv : the preprint server for biology

2024

Abstract: The evolution of multicellularity paved the way for the origin of complex life on Earth, but little is known about the mechanistic basis of early multicellular evolution. Here, we examine the molecular basis of multicellular adaptation in the ... ...

Abstract	The evolution of multicellularity paved the way for the origin of complex life on Earth, but little is known about the mechanistic basis of early multicellular evolution. Here, we examine the molecular basis of multicellular adaptation in the Multicellularity Long Term Evolution Experiment (MuLTEE). We demonstrate that cellular elongation, a key adaptation underpinning increased biophysical toughness and organismal size, is convergently driven by downregulation of the chaperone Hsp90. Mechanistically, Hsp90-mediated morphogenesis operates by destabilizing the cyclin-dependent kinase Cdc28, resulting in delayed mitosis and prolonged polarized growth. Reinstatement of Hsp90 or Cdc28 expression resulted in shortened cells that formed smaller groups with reduced multicellular fitness. Together, our results show how ancient protein folding systems can be tuned to drive rapid evolution at a new level of biological individuality by revealing novel developmental phenotypes.
Language	English
Publishing date	2024-01-22
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.05.31.543183
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Article ; Online: Proteostatic tuning underpins the evolution of novel multicellular traits.

Montrose, Kristopher / Lac, Dung T / Burnetti, Anthony J / Tong, Kai / Bozdag, G Ozan / Hukkanen, Mikaela / Ratcliff, William C / Saarikangas, Juha

Science advances

2024 Volume 10, Issue 10, Page(s) eadn2706

Abstract	The evolution of multicellularity paved the way for the origin of complex life on Earth, but little is known about the mechanistic basis of early multicellular evolution. Here, we examine the molecular basis of multicellular adaptation in the multicellularity long-term evolution experiment (MuLTEE). We demonstrate that cellular elongation, a key adaptation underpinning increased biophysical toughness and organismal size, is convergently driven by down-regulation of the chaperone Hsp90. Mechanistically, Hsp90-mediated morphogenesis operates by destabilizing the cyclin-dependent kinase Cdc28, resulting in delayed mitosis and prolonged polarized growth. Reinstatement of Hsp90 or Cdc28 expression resulted in shortened cells that formed smaller groups with reduced multicellular fitness. Together, our results show how ancient protein folding systems can be tuned to drive rapid evolution at a new level of biological individuality by revealing novel developmental phenotypes.
MeSH term(s)	Biological Evolution ; HSP90 Heat-Shock Proteins/metabolism ; Mitosis ; Protein Folding ; Phenotype
Chemical Substances	HSP90 Heat-Shock Proteins
Language	English
Publishing date	2024-03-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adn2706
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Article ; Online: Actin-rich lamellipodia-like protrusions contribute to the integrity of epithelial cell-cell junctions.

Senju, Yosuke / Mushtaq, Toiba / Vihinen, Helena / Manninen, Aki / Saarikangas, Juha / Ven, Katharina / Engel, Ulrike / Varjosalo, Markku / Jokitalo, Eija / Lappalainen, Pekka

The Journal of biological chemistry

2023 Volume 299, Issue 5, Page(s) 104571

Abstract: Metastasis-suppressor 1 (MTSS1) is a membrane-interacting scaffolding protein that regulates the integrity of epithelial cell-cell junctions and functions as a tumor suppressor in a wide range of carcinomas. MTSS1 binds phosphoinositide-rich membranes ... ...

Abstract	Metastasis-suppressor 1 (MTSS1) is a membrane-interacting scaffolding protein that regulates the integrity of epithelial cell-cell junctions and functions as a tumor suppressor in a wide range of carcinomas. MTSS1 binds phosphoinositide-rich membranes through its I-BAR domain and is capable of sensing and generating negative membrane curvature in vitro. However, the mechanisms by which MTSS1 localizes to intercellular junctions in epithelial cells and contributes to their integrity and maintenance have remained elusive. By carrying out EM and live-cell imaging on cultured Madin-Darby canine kidney cell monolayers, we provide evidence that adherens junctions of epithelial cells harbor lamellipodia-like, dynamic actin-driven membrane folds, which exhibit high negative membrane curvature at their distal edges. BioID proteomics and imaging experiments demonstrated that MTSS1 associates with an Arp2/3 complex activator, the WAVE-2 complex, in dynamic actin-rich protrusions at cell-cell junctions. Inhibition of Arp2/3 or WAVE-2 suppressed actin filament assembly at adherens junctions, decreased the dynamics of junctional membrane protrusions, and led to defects in epithelial integrity. Together, these results support a model in which membrane-associated MTSS1, together with the WAVE-2 and Arp2/3 complexes, promotes the formation of dynamic lamellipodia-like actin protrusions that contribute to the integrity of cell-cell junctions in epithelial monolayers.
MeSH term(s)	Animals ; Dogs ; Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Adherens Junctions/metabolism ; Epithelial Cells/metabolism ; Intercellular Junctions/metabolism ; Madin Darby Canine Kidney Cells ; Membrane Proteins/metabolism ; Pseudopodia/metabolism ; Microfilament Proteins/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; Membrane Proteins ; Microfilament Proteins
Language	English
Publishing date	2023-03-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104571
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Article ; Online: Spatial regulation of coalesced protein assemblies: Lessons from yeast to diseases.

Saarikangas, Juha / Caudron, Fabrice

Prion

2017 Volume 11, Issue 3, Page(s) 162–173

Abstract: Organisms rely on correctly folded proteins to carry out essential functions. Protein quality control factors guard proteostasis and prevent protein misfolding. When quality control fails and in response to diverse stresses, many proteins start to ... ...

Abstract	Organisms rely on correctly folded proteins to carry out essential functions. Protein quality control factors guard proteostasis and prevent protein misfolding. When quality control fails and in response to diverse stresses, many proteins start to accumulate at specific deposit sites that maintain cellular organization and protect the functionality of coalescing proteins. These transitions involve dedicated proteins that promote coalescence and are facilitated by endo-membranes and cytoskeletal platforms. Moreover, several proteins make use of weak multivalent interactions or conformational templating to drive the formation of large-scale assemblies. Formation of such assemblies is often associated with a change in biochemical activity that can be used by cells to execute biochemical decisions in a localized manner during development and adaption. Since all assembly types impact cell physiology, their localization and dynamics need to be tightly regulated. Interestingly, at least some of the regulatory mechanisms are shared by functional membrane-less organelles and assemblies of terminally aggregated proteins. Furthermore, constituents of functional assemblies can aggregate and become non-functional during aging. Here we present the current knowledge as to how coalescing protein assemblies are spatially organized in cells and we postulate that failures in their spatial confinement might underscore certain aspects of aging and neurodegenerative diseases.
MeSH term(s)	Aging/physiology ; Humans ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Neurodegenerative Diseases/physiopathology ; Proteins/chemistry ; Proteins/metabolism ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Multiprotein Complexes ; Proteins
Language	English
Publishing date	2017-06-02
Publishing country	United States
Document type	Journal Article
ISSN	1933-690X
ISSN (online)	1933-690X
DOI	10.1080/19336896.2017.1322239
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Article ; Online: Winter is coming: Regulation of cellular metabolism by enzyme polymerization in dormancy and disease.

Montrose, Kristopher / López Cabezas, Rosa María / Paukštytė, Jurgita / Saarikangas, Juha

Experimental cell research

2020 Volume 397, Issue 2, Page(s) 112383

Abstract: Metabolism feeds growth. Accordingly, metabolism is regulated by nutrient-sensing pathways that converge growth promoting signals into biosynthesis by regulating the activity of metabolic enzymes. When the environment does not support growth, organisms ... ...

Abstract	Metabolism feeds growth. Accordingly, metabolism is regulated by nutrient-sensing pathways that converge growth promoting signals into biosynthesis by regulating the activity of metabolic enzymes. When the environment does not support growth, organisms invest in survival. For cells, this entails transitioning into a dormant, quiescent state (G0). In dormancy, the activity of biosynthetic pathways is dampened, and catabolic metabolism and stress tolerance pathways are activated. Recent work in yeast has demonstrated that dormancy is associated with alterations in the physicochemical properties of the cytoplasm, including changes in pH, viscosity and macromolecular crowding. Accompanying these changes, numerous metabolic enzymes transition from soluble to polymerized assemblies. These large-scale self-assemblies are dynamic and depolymerize when cells resume growth. Here we review how enzyme polymerization enables metabolic plasticity by tuning carbohydrate, nucleic acid, amino acid and lipid metabolic pathways, with particular focus on its potential adaptive value in cellular dormancy.
MeSH term(s)	Animals ; Cell Physiological Phenomena ; Disease ; Enzymes/chemistry ; Enzymes/metabolism ; Humans ; Metabolic Networks and Pathways ; Polymerization
Chemical Substances	Enzymes
Language	English
Publishing date	2020-11-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2020.112383
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Article: The initiation of post-synaptic protrusions.

Hotulainen, Pirta / Saarikangas, Juha

Communicative & integrative biology

2016 Volume 9, Issue 3, Page(s) e1125053

Abstract: The post-synaptic spines of neuronal dendrites are highly elaborate membrane protrusions. Their anatomy, stability and density are intimately linked to cognitive performance. The morphological transitions of spines are powered by coordinated ... ...

Abstract	The post-synaptic spines of neuronal dendrites are highly elaborate membrane protrusions. Their anatomy, stability and density are intimately linked to cognitive performance. The morphological transitions of spines are powered by coordinated polymerization of actin filaments against the plasma membrane, but how the membrane-associated polymerization is spatially and temporally regulated has remained ill defined. Here, we discuss our recent findings showing that dendritic spines can be initiated by direct membrane bending by the I-BAR protein MIM/Mtss1. This lipid phosphatidylinositol (PI(4,5)P2) signaling-activated membrane bending coordinated spatial actin assembly and promoted spine formation. From recent advances, we formulate a general model to discuss how spatially concentrated protein-lipid microdomains formed by multivalent interactions between lipids and actin/membrane regulatory proteins might launch cell protrusions.
Language	English
Publishing date	2016-04-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2451097-X
ISSN	1942-0889
ISSN	1942-0889
DOI	10.1080/19420889.2015.1125053
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Article ; Online: Protein aggregation as a mechanism of adaptive cellular responses.

Saarikangas, Juha / Barral, Yves

Current genetics

2016 Volume 62, Issue 4, Page(s) 711–724

Abstract: Coalescence of proteins into different types of intracellular bodies has surfaced as a widespread adaptive mechanism to re-organize cells and cellular functions in response to specific cues. These structures, composed of proteins or protein-mRNA- ... ...

Abstract	Coalescence of proteins into different types of intracellular bodies has surfaced as a widespread adaptive mechanism to re-organize cells and cellular functions in response to specific cues. These structures, composed of proteins or protein-mRNA-complexes, regulate cellular processes through modulating enzymatic activities, gene expression or shielding macromolecules from damage. Accordingly, such bodies are associated with a wide-range of processes, including meiosis, memory-encoding, host-pathogen interactions, cancer, stress responses, as well as protein quality control, DNA replication stress and aneuploidy. Importantly, these distinct coalescence responses are controlled, and in many cases regulated by chaperone proteins. While cells can tolerate and proficiently coordinate numerous distinct types of protein bodies, some of them are also intimately linked to diseases or the adverse effects of aging. Several protein bodies that differ in composition, packing, dynamics, size, and localization were originally discovered in budding yeast. Here, we provide a concise and comparative review of their nature and nomenclature.
MeSH term(s)	Adaptation, Physiological ; Aging/metabolism ; Cytoplasmic Granules ; Gene Expression ; Humans ; Prions/chemistry ; Prions/metabolism ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Transport ; Proteins/chemistry ; Proteins/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Stress, Physiological ; Yeasts/genetics ; Yeasts/metabolism
Chemical Substances	Prions ; Protein Aggregates ; Proteins ; RNA, Messenger ; RNA-Binding Proteins
Language	English
Publishing date	2016-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-016-0596-0
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Article ; Online: Preparing junior faculty for success.

Sawarkar, Ritwick / Scherz-Shouval, Ruth / Denzel, Martin / Saarikangas, Juha

Science (New York, N.Y.)

2018 Volume 361, Issue 6399, Page(s) 238

Language	English
Publishing date	2018-07-19
Publishing country	United States
Document type	Letter
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aau4531
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Article ; Online: A rare natural lipid induces neuroglobin expression to prevent amyloid oligomers toxicity and retinal neurodegeneration.

Oamen, Henry Patrick / Romero Romero, Nathaly / Knuckles, Philip / Saarikangas, Juha / Radman-Livaja, Marta / Dong, Yuhong / Caudron, Fabrice

Aging cell

2022 Volume 21, Issue 7, Page(s) e13645

Abstract: Most neurodegenerative diseases such as Alzheimer's disease are proteinopathies linked to the toxicity of amyloid oligomers. Treatments to delay or cure these diseases are lacking. Using budding yeast, we report that the natural lipid tripentadecanoin ... ...

Abstract	Most neurodegenerative diseases such as Alzheimer's disease are proteinopathies linked to the toxicity of amyloid oligomers. Treatments to delay or cure these diseases are lacking. Using budding yeast, we report that the natural lipid tripentadecanoin induces expression of the nitric oxide oxidoreductase Yhb1 to prevent the formation of protein aggregates during aging and extends replicative lifespan. In mammals, tripentadecanoin induces expression of the Yhb1 orthologue, neuroglobin, to protect neurons against amyloid toxicity. Tripentadecanoin also rescues photoreceptors in a mouse model of retinal degeneration and retinal ganglion cells in a Rhesus monkey model of optic atrophy. Together, we propose that tripentadecanoin affects p-bodies to induce neuroglobin expression and offers a potential treatment for proteinopathies and retinal neurodegeneration.
MeSH term(s)	Animals ; Mice ; Alzheimer Disease ; Amyloid/drug effects ; Amyloid/metabolism ; Amyloid beta-Peptides/drug effects ; Amyloid beta-Peptides/metabolism ; Dioxygenases ; Hemeproteins ; Lipids/pharmacology ; Mammals ; Neuroglobin/drug effects ; Neuroglobin/metabolism ; Processing Bodies/drug effects ; Processing Bodies/metabolism ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/metabolism ; Retinal Ganglion Cells/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Dioxygenases (EC 1.13.11.-) ; Hemeproteins ; Lipids ; Neuroglobin ; Saccharomyces cerevisiae Proteins ; YHB1 protein, S cerevisiae (EC 1.14.12.17) ; tripentadecanoin
Language	English
Publishing date	2022-06-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.13645
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