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  • 1
    Language: English
    In: The Journal of cell biology, 2017-09-04, Vol.216 (9), p.2623-2632
    Description: Cell surface receptor uptake via clathrin-mediated endocytosis (CME) and subsequent intracellular sorting for degradation or recycling regulates the strength and specificity of downstream signaling. Signaling, in turn, modulates early endocytic trafficking. This reciprocal regulation of signaling and endocytosis provides opportunities for the establishment of feedback loops to enhance or suppress surface-derived signals. Recent studies suggest that dynamin-1, a presumed neuron-specific isoform of the large, membrane fission GTPase, can be activated in nonneuronal cells downstream of cancer-relevant signaling pathways and thereby function as a nexus between signaling and early endocytic trafficking. I speculate that sustained up-regulation and/or acute activation of dynamin-1 in cancer cells contributes to a program of "adaptive" CME that alters signaling to enhance cancer cell survival, migration, and proliferation.
    Subject(s): Neoplasms - metabolism ; Cell Proliferation ; Signal Transduction ; Humans ; Receptors, Cell Surface - metabolism ; Clathrin-Coated Vesicles - metabolism ; Protein Transport ; Endocytosis ; Feedback, Physiological ; Animals ; Dynamin I - metabolism ; Neoplasms - pathology ; Cell Movement ; Cell research ; Cancer cells ; Cellular control mechanisms ; Physiological aspects ; Cellular signal transduction ; Research ; Index Medicus ; Reviews
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 2
    Language: English
    In: European journal of immunology, 2015-10, Vol.45 (10), p.2911-2917
    Description: Inflammasome activation culminates in activation of caspase‐1, which leads to the maturation and subsequent release of cytokines of the interleukin 1 (IL‐1) family and results in a particular form of cell death known as pyroptosis. In addition, in the murine system, a so‐called non‐canonical inflammasome involving caspase‐11 has been described that directly responds to cytosolic LPS. Here, we show that the human monocytic cell line THP1 activates the inflammasome in response to cytosolic LPS in a TLR4‐independent fashion. This response is mediated by caspase‐4 and accompanied by caspase‐1 activation, pyroptosis, and IL‐1β maturation. In addition to caspase‐4, efficient IL‐1β conversion upon intracellular LPS delivery relies on potassium efflux, NLRP3, ASC, and caspase‐1, indicating that although caspase‐4 activation alone is sufficient to induce pyroptosis, this process depends on the NLRP3 inflammasome activation to drive IL‐1β maturation. Altogether, this study provides evidence for the presence of a non‐canonical inflammasome in humans and its dependence on caspase‐4.
    Subject(s): Non‐canonical inflammasome ; NLRP3 ; Myeloid cells ; Caspase‐4 ; Myeloid Cells - cytology ; Caspases, Initiator - immunology ; NLR Family, Pyrin Domain-Containing 3 Protein ; Humans ; Interleukin-1beta - immunology ; Caspase 1 - immunology ; Interleukin-1beta - genetics ; Caspases, Initiator - genetics ; Enzyme Activation - drug effects ; Inflammasomes - genetics ; Carrier Proteins - genetics ; Caspase 1 - genetics ; Myeloid Cells - immunology ; Inflammasomes - immunology ; Lipopolysaccharides - pharmacology ; Cell Line, Tumor ; Carrier Proteins - immunology ; Interleukins ; Cell death ; Index Medicus
    ISSN: 0014-2980
    E-ISSN: 1521-4141
    Source: Alma/SFX Local Collection
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  • 3
    Article
    Article
    2003
    ISSN: 0028-0836 
    Language: English
    In: Nature (London), 2003-03-06, Vol.422 (6927), p.37-44
    Description: The plasma membrane is the interface between cells and their harsh environment. Uptake of nutrients and all communication among cells and between cells and their environment occurs through this interface. 'Endocytosis' encompasses several diverse mechanisms by which cells internalize macromolecules and particles into transport vesicles derived from the plasma membrane. It controls entry into the cell and has a crucial role in development, the immune response, neurotransmission, intercellular communication, signal transduction, and cellular and organismal homeostasis. As the complexity of molecular interactions governing endocytosis are revealed, it has become increasingly clear that it is tightly coordinated and coupled with overall cell physiology and thus, must be viewed in a broader context than simple vesicular trafficking.
    Subject(s): Fundamental and applied biological sciences. Psychology ; Biological and medical sciences ; Molecular and cellular biology ; Protein Kinases - metabolism ; Dynamins - metabolism ; Actins - metabolism ; Lipid Metabolism ; Pinocytosis ; Caveolins - metabolism ; Clathrin - metabolism ; Cells - enzymology ; Endocytosis ; Animals ; Caveolin 1 ; Biological Transport ; Cells - metabolism ; Cell Membrane - metabolism ; Cells - cytology ; Index Medicus
    ISSN: 0028-0836
    E-ISSN: 1476-4687
    Source: Nature Journal Archive
    Source: Academic Search Ultimate
    Source: Nature Journals Online
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 4
    Language: English
    In: Science (American Association for the Advancement of Science), 2009-09-04, Vol.325 (5945), p.1217-1220
    Description: Coated vesicles concentrate and package cargo molecules to mediate their efficient transport between intracellular compartments. Cytosolic coat proteins such as clathrin and adaptor complexes and coat protein complex I (COPI) and COPII self-assemble to deform the membrane and interact directly with cargo molecules to capture them in nascent buds. The guanosine tríphosphatases (GTPases) Art, Sar1, and dynamin are core components of the coated vesicle machinery. These GTPases, which associate with and dissociate from donor membranes in a guanosine triphosphate—dependent manner, can also actively remodel membranes. Recent evidence suggests that, although structurally diverse, Arf family GTPases and dynamin may play mechanistically similar roles as fidelity monitors that govern cargo packaging and coated vesicle maturation and as components of the fission machinery to mediate vesicle release.
    Subject(s): Hydrolysis ; Proteins ; Molecules ; Rock cleavage ; Coated vesicles ; Freight transport ; Cell membranes ; Review ; Curvature ; Freight ; P branes ; Fundamental and applied biological sciences. Psychology ; Biological and medical sciences ; Cell physiology ; Molecular and cellular biology ; Membrane and intracellular transports ; COP-Coated Vesicles - ultrastructure ; Clathrin-Coated Vesicles - chemistry ; Dynamins - metabolism ; Vesicular Transport Proteins - metabolism ; Humans ; COP-Coated Vesicles - metabolism ; Cell Membrane - ultrastructure ; Guanosine Triphosphate - metabolism ; COP-Coated Vesicles - chemistry ; Clathrin-Coated Vesicles - metabolism ; Animals ; GTP Phosphohydrolases - metabolism ; Dynamins - chemistry ; Monomeric GTP-Binding Proteins - metabolism ; Guanine Nucleotide Exchange Factors - metabolism ; Monomeric GTP-Binding Proteins - chemistry ; ADP-Ribosylation Factor 1 - metabolism ; Protein Conformation ; Cell Membrane - metabolism ; Clathrin-Coated Vesicles - ultrastructure ; Guanosine Diphosphate - metabolism ; ADP-Ribosylation Factor 1 - chemistry ; Clathrin-coated vesicles ; Biological transport ; Physiological aspects ; Research ; Properties ; Guanosine triphosphatase ; Membrane proteins ; Index Medicus
    ISSN: 0036-8075
    E-ISSN: 1095-9203
    Source: Single Journals
    Source: Academic Search Ultimate
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 5
    Language: English
    In: Science (American Association for the Advancement of Science), 2013-03-22, Vol.339 (6126), p.1433-1436
    Description: Biological membrane fission requires protein-driven stress. The guanosine triphosphatase (GTPase) dynamin builds up membrane stress by polymerizing into a helical collar that constricts the neck of budding vesicles. How this curvature stress mediates nonleaky membrane remodeling is actively debated. Using lipid nanotubes as substrates to directly measure geometric intermediates of the fission pathway, we found that GTP hydrolysis limits dynamin polymerization into short, metastable collars that are optimal for fission. Collars as short as two rungs translated radial constriction to reversible hemifission via membrane wedging of the pleckstrin homology domains (PHDs) of dynamin. Modeling revealed that tilting of the PHDs to conform with membrane deformations creates the low-energy pathway for hemifission. This local coordination of dynamin and lipids suggests how membranes can be remodeled in cells.
    Subject(s): Hydrolysis ; REPORTS ; Fluorescence ; Lipids ; Mathematical rings ; Catalysis ; Movies ; Remodeling ; Scaffolds ; Curvature ; P branes ; Protein Structure, Tertiary ; Biocatalysis ; Protein Multimerization ; Nanotubes ; Guanosine Triphosphate - metabolism ; Thermodynamics ; Models, Biological ; Dynamin I - chemistry ; Dynamin I - metabolism ; Protein Conformation ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Physiological aspects ; Polymerization ; Research ; Membranes (Biology) ; Guanosine triphosphatase ; Index Medicus
    ISSN: 0036-8075
    E-ISSN: 1095-9203
    Source: Single Journals
    Source: Academic Search Ultimate
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 6
    Language: English
    In: Immunity (Cambridge, Mass.), 2016-04-19, Vol.44 (4), p.833-846
    Description: Interleukin-1β (IL-1β) is a cytokine whose bioactivity is controlled by activation of the inflammasome. However, in response to lipopolysaccharide, human monocytes secrete IL-1β independently of classical inflammasome stimuli. Here, we report that this constituted a species-specific response that is not observed in the murine system. Indeed, in human monocytes, lipopolysaccharide triggered an “alternative inflammasome” that relied on NLRP3-ASC-caspase-1 signaling, yet was devoid of any classical inflammasome characteristics including pyroptosome formation, pyroptosis induction, and K+ efflux dependency. Genetic dissection of the underlying signaling pathway in a monocyte transdifferentiation system revealed that alternative inflammasome activation was propagated by TLR4-TRIF-RIPK1-FADD-CASP8 signaling upstream of NLRP3. Importantly, involvement of this signaling cascade was limited to alternative inflammasome activation and did not extend to classical NLRP3 activation. Because alternative inflammasome activation embraces both sensitivity and promiscuity of TLR4, we propose a pivotal role for this signaling cascade in TLR4-driven, IL-1β-mediated immune responses and immunopathology in humans. [Display omitted] •LPS by itself triggers IL-1β secretion in human, but not in murine monocytes•Human monocytes activate an alternative inflammasome in response to LPS•This proceeds independently of K+ efflux, pyroptosome formation, and pyroptosis•Alternative but not classical inflammasome signals via TLR4-TRIF-RIPK1-FADD-CASP8 How human monocytes secrete processed IL-1β upon LPS challenge is unknown. Hornung and colleagues report that LPS triggers an alternative NLRP3 inflammasome pathway in human monocytes. Unlike classical NLRP3 inflammasome signaling, alternative inflammasome activation proceeds independently of potassium efflux, pyroptosome formation, and pyroptosis, while it engages TLR4-TRIF-RIPK1-FADD-CASP8 upstream of NLRP3.
    Subject(s): Interleukin-1beta - secretion ; Potassium - metabolism ; Cell Line ; NLR Family, Pyrin Domain-Containing 3 Protein ; Humans ; Potassium Channels - immunology ; Interleukin-1beta - immunology ; Caspase 1 - immunology ; Monocytes - immunology ; Toll-Like Receptor 4 - immunology ; Cell Transdifferentiation - immunology ; Lipopolysaccharides ; Signal Transduction - immunology ; Animals ; Inflammasomes - immunology ; Mice ; Carrier Proteins - immunology ; Pyroptosis - immunology ; Interleukins ; Mitogens ; Index Medicus
    ISSN: 1074-7613
    E-ISSN: 1097-4180
    Source: Backfile Package - All of Back Files EBS [ALLOFBCKF]
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 7
    Language: English
    In: The Journal of cell biology, 2010-03-22, Vol.188 (6), p.919-933
    Description: Clathrin-mediated endocytosis of surface receptors and their bound ligands (i.e., cargo) is highly regulated, including by the cargo itself. One of the possible sources of the observed heterogeneous dynamics of clathrin-coated pits (CCPs) might be the different cargo content. Consistent with this, we show that CCP size and dynamic behavior varies with low density lipoprotein receptor (LDLR) expression levels in a manner dependent on the LDLR-specific adaptors, Dab2 and ARH. In Dab2-mCherry—expressing cells, varying LDLR expression leads to a progressive increase in CCP size and to the appearance of nonterminal endocytic events. In LDLR and ARH-mCherry—expressing cells in addition to an increase in CCP size, turnover of abortive CCPs increases, and the rate of CCP maturation decreases. Altogether, our results underscore the highly dynamic and cargo-responsive nature of CCP assembly and suggest that the observed heterogeneity is, in part, related to compositional differences (e.g., cargo and adaptors) between CCPs.
    Subject(s): Endocytosis ; Receptors ; Adenoviruses ; Cell lines ; Antibodies ; Cell membranes ; Kidney cells ; Physiological regulation ; Chimeras ; Freight ; Particle Size ; Coated Pits, Cell-Membrane - metabolism ; Animals ; Time Factors ; Cells, Cultured ; Cercopithecus aethiops ; Rats ; Receptors, LDL - metabolism ; Ligands ; Adaptor Proteins, Signal Transducing - metabolism ; Clathrin - metabolism ; Clathrin ; Research ; Properties ; Index Medicus
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 8
    Language: English
    In: The Journal of cell biology, 2010-12-27, Vol.191 (7), p.1381-1393
    Description: Clathrin-mediated endocytosis (CME) is the major pathway for concentrative uptake of receptors and receptor—ligand complexes (cargo). Although constitutively internalized cargos are known to accumulate into maturing clathrin-coated pits (CCPs), whether and how cargo recruitment affects the initiation and maturation of CCPs is not fully understood. Previous studies have addressed these issues by analyzing the global effects of receptor overexpression on CME or CCP dynamics. Here, we exploit a refined approach using expression of a biotinylated transferrin receptor (bTfnR) and controlling its local clustering using mono- or multivalent streptavidin. We show that local clustering of bTfnR increased CCP initiation. By tracking cargo loading in individual CCPs, we found that bTfnR clustering preceded clathrin assembly and confirmed that bTfnR-containing CCPs mature more efficiently than bTfnR-free CCPs. Although neither the clustering nor the related changes in cargo loading altered the rate of CCP maturation, bTfnR-containing CCPs exhibited significantly longer lifetimes than other CCPs within the same cell. Together these results demonstrate that cargo composition is a key source of the differential dynamics of CCPs.
    Subject(s): Molecules ; Receptors ; Endocytosis ; Internalization ; Imaging ; Fluorescence ; Ligands ; Physiological regulation ; Freight ; Transferrin receptors ; Coated Pits, Cell-Membrane - ultrastructure ; Humans ; Cercopithecus aethiops ; Recombinant Fusion Proteins - metabolism ; Carbon-Nitrogen Ligases - genetics ; Adaptor Protein Complex sigma Subunits - metabolism ; Coated Pits, Cell-Membrane - physiology ; Epithelial Cells - physiology ; Adaptor Protein Complex 2 - metabolism ; Clathrin Light Chains - metabolism ; Biotin - metabolism ; Cell Membrane - metabolism ; Receptors, Transferrin - genetics ; Clathrin Light Chains - genetics ; Epithelial Cells - cytology ; Biotinylation - genetics ; Cell Line ; Transduction, Genetic ; Rats ; Repressor Proteins - genetics ; Adaptor Protein Complex 2 - genetics ; Adaptor Protein Complex sigma Subunits - genetics ; Receptors, Transferrin - metabolism ; Streptavidin - genetics ; Endocytosis - physiology ; Receptor Aggregation - physiology ; Animals ; Streptavidin - metabolism ; Escherichia coli Proteins - genetics ; Recombinant Fusion Proteins - genetics ; Biotinylation - methods ; Kinetics ; Protein Binding - physiology ; Transferrin ; Cell receptors ; Clathrin ; Research ; Properties ; Index Medicus ; s
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 9
    Language: English
    In: Trends in cell biology, 2016, Vol.27 (3), p.189-200
    Description: Sorting nexin (SNX)9 was first discovered as an endocytic accessory protein involved in clathrin-mediated endocytosis. However, recent data suggest that SNX9 is a multifunctional scaffold that coordinates membrane trafficking and remodeling with changes in actin dynamics to affect diverse cellular processes. Here, we review the accumulated knowledge on SNX9 with an emphasis on its recently identified roles in clathrin-independent endocytic pathways, cell invasion, and cell division, which have implications for SNX9 function in human disease, including cancer.
    Subject(s): Pathology
    ISSN: 0962-8924
    E-ISSN: 1879-3088
    Source: Backfile Package - All of Back Files EBS [ALLOFBCKF]
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  • 10
    Language: English
    In: The Journal of cell biology, 2020-09-07, Vol.219 (9)
    Description: Clathrin-mediated endocytosis occurs via the assembly of clathrin-coated pits (CCPs) that invaginate and pinch off to form clathrin-coated vesicles (CCVs). It is well known that adaptor protein 2 (AP2) complexes trigger clathrin assembly on the plasma membrane, and biochemical and structural studies have revealed the nature of these interactions. Numerous endocytic accessory proteins collaborate with clathrin and AP2 to drive CCV formation. However, many questions remain as to the molecular events involved in CCP initiation, stabilization, and curvature generation. Indeed, a plethora of recent evidence derived from cell perturbation, correlative light and EM tomography, live-cell imaging, modeling, and high-resolution structural analyses has revealed more complexity and promiscuity in the protein interactions driving CCP maturation than anticipated. After briefly reviewing the evidence supporting prevailing models, we integrate these new lines of evidence to develop a more dynamic and flexible model for how redundant, dynamic, and competing protein interactions can drive endocytic CCV formation and suggest new approaches to test emerging models.
    Subject(s): Coated Pits, Cell-Membrane - metabolism ; Adaptor Protein Complex 2 - metabolism ; Humans ; Cell Membrane - metabolism ; Cell Membrane - physiology ; Clathrin - metabolism ; Clathrin-Coated Vesicles - metabolism ; Coated Pits, Cell-Membrane - physiology ; Endocytosis - physiology ; Index Medicus
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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