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  • 1
    Online Resource
    Online Resource
    Differential PI 3-kinase dependence of early and late phases of recycling of the internalized AT1 angiotensin receptor
    Rockefeller University Press ; 2002
    In:  The Journal of Cell Biology Vol. 157, No. 7 ( 2002-06-24), p. 1211-1222
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 157, No. 7 ( 2002-06-24), p. 1211-1222
    Abstract: Agonist-induced endocytosis and processing of the G protein–coupled AT1 angiotensin II (Ang II) receptor (AT1R) was studied in HEK 293 cells expressing green fluorescent protein (GFP)– or hemagglutinin epitope–tagged forms of the receptor. After stimulation with Ang II, the receptor and its ligand colocalized with Rab5–GFP and Rab4–GFP in early endosomes, and subsequently with Rab11–GFP in pericentriolar recycling endosomes. Inhibition of phosphatidylinositol (PI) 3-kinase by wortmannin (WT) or LY294002 caused the formation of large endosomal vesicles of heterogeneous Rab composition, containing the ligand–receptor complex in their limiting membranes and in small associated vesicular structures. In contrast to Alexa®–transferrin, which was mainly found in small vesicles associated with the outside of large vesicles in WT-treated cells, rhodamine–Ang II was also segregated into small internal vesicles. In cells labeled with 125I-Ang II, WT treatment did not impair the rate of receptor endocytosis, but significantly reduced the initial phase of receptor recycling without affecting its slow component. Similarly, WT inhibited the early, but not the slow, component of the recovery of AT1R at the cell surface after termination of Ang II stimulation. These data indicate that internalized AT1 receptors are processed via vesicles that resemble multivesicular bodies, and recycle to the cell surface by a rapid PI 3-kinase–dependent recycling route, as well as by a slower pathway that is less sensitive to PI 3-kinase inhibitors.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200111013
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2002
    detail.hit.zdb_id: 1421310-2
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  • 2
    Online Resource
    Online Resource
    Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    Rockefeller University Press ; 2001
    In:  The Journal of Cell Biology Vol. 154, No. 5 ( 2001-09-03), p. 1007-1018
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 154, No. 5 ( 2001-09-03), p. 1007-1018
    Abstract: ADP-ribosylation factor (Arf) 6 regulates the movement of membrane between the plasma membrane (PM) and a nonclathrin-derived endosomal compartment and activates phosphatidylinositol 4-phosphate 5-kinase (PIP 5-kinase), an enzyme that generates phosphatidylinositol 4,5-bisphosphate (PIP2). Here, we show that PIP2 visualized by expressing a fusion protein of the pleckstrin homology domain from PLCδ and green fluorescent protein (PH-GFP), colocalized with Arf6 at the PM and on tubular endosomal structures. Activation of Arf6 by expression of its exchange factor EFA6 stimulated protrusion formation, the uptake of PM into macropinosomes enriched in PIP2, and recycling of this membrane back to the PM. By contrast, expression of Arf6 Q67L, a GTP hydrolysis-resistant mutant, induced the formation of PIP2-positive actin-coated vacuoles that were unable to recycle membrane back to the PM. PM proteins, such as β1-integrin, plakoglobin, and major histocompatibility complex class I, that normally traffic through the Arf6 endosomal compartment became trapped in this vacuolar compartment. Overexpression of human PIP 5-kinase α mimicked the effects seen with Arf6 Q67L. These results demonstrate that PIP 5-kinase activity and PIP2 turnover controlled by activation and inactivation of Arf6 is critical for trafficking through the Arf6 PM-endosomal recycling pathway.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200103107
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2001
    detail.hit.zdb_id: 1421310-2
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  • 3
    Online Resource
    Online Resource
    Structural and functional features and significance of the physical linkage between ER and mitochondria
    Rockefeller University Press ; 2006
    In:  The Journal of Cell Biology Vol. 174, No. 7 ( 2006-09-25), p. 915-921
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 174, No. 7 ( 2006-09-25), p. 915-921
    Abstract: The role of mitochondria in cell metabolism and survival is controlled by calcium signals that are commonly transmitted at the close associations between mitochondria and endoplasmic reticulum (ER). However, the physical linkage of the ER–mitochondria interface and its relevance for cell function remains elusive. We show by electron tomography that ER and mitochondria are adjoined by tethers that are ∼10 nm at the smooth ER and ∼25 nm at the rough ER. Limited proteolysis separates ER from mitochondria, whereas expression of a short “synthetic linker” ( & lt;5 nm) leads to tightening of the associations. Although normal connections are necessary and sufficient for proper propagation of ER-derived calcium signals to the mitochondria, tightened connections, synthetic or naturally observed under apoptosis-inducing conditions, make mitochondria prone to Ca2+ overloading and ensuing permeability transition. These results reveal an unexpected dependence of cell function and survival on the maintenance of proper spacing between the ER and mitochondria.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200604016
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2006
    detail.hit.zdb_id: 1421310-2
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  • 4
    Online Resource
    Online Resource
    Defining the subcellular distribution and metabolic channeling of phosphatidylinositol
    Rockefeller University Press ; 2020
    In:  Journal of Cell Biology Vol. 219, No. 3 ( 2020-03-02)
    Details
    In: Journal of Cell Biology, Rockefeller University Press, Vol. 219, No. 3 ( 2020-03-02)
    Abstract: Phosphatidylinositol (PI) is an essential structural component of eukaryotic membranes that also serves as the common precursor for polyphosphoinositide (PPIn) lipids. Despite the recognized importance of PPIn species for signal transduction and membrane homeostasis, there is still a limited understanding of the relationship between PI availability and the turnover of subcellular PPIn pools. To address these shortcomings, we established a molecular toolbox for investigations of PI distribution within intact cells by exploiting the properties of a bacterial enzyme, PI-specific PLC (PI-PLC). Using these tools, we find a minor presence of PI in membranes of the ER, as well as a general enrichment within the cytosolic leaflets of the Golgi complex, peroxisomes, and outer mitochondrial membrane, but only detect very low steady-state levels of PI within the plasma membrane (PM) and endosomes. Kinetic studies also demonstrate the requirement for sustained PI supply from the ER for the maintenance of monophosphorylated PPIn species within the PM, Golgi complex, and endosomal compartments.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.201906130
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2020
    detail.hit.zdb_id: 1421310-2
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  • 5
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    Online Resource
    Rushing to maintain plasma membrane phosphoinositide levels
    Rockefeller University Press ; 2020
    In:  Journal of General Physiology Vol. 152, No. 12 ( 2020-12-07)
    Details
    In: Journal of General Physiology, Rockefeller University Press, Vol. 152, No. 12 ( 2020-12-07)
    Abstract: New findings by Myeong et al. provide further details on how cells maintain their plasma membrane PI(4,5)P2 levels when stimulated via M1 muscarinic receptors
    Type of Medium: Online Resource
    ISSN: 0022-1295 , 1540-7748
    URL: Article
    DOI: 10.1085/jgp.202012793
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2020
    detail.hit.zdb_id: 1477246-2
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  • 6
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    Online Resource
    Restricted Accumulation of Phosphatidylinositol 3-Kinase Products in a Plasmalemmal Subdomain during Fcγ Receptor-Mediated Phagocytosis
    Rockefeller University Press ; 2001
    In:  The Journal of Cell Biology Vol. 153, No. 7 ( 2001-06-25), p. 1369-1380
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 153, No. 7 ( 2001-06-25), p. 1369-1380
    Abstract: Phagocytosis is a highly localized and rapid event, requiring the generation of spatially and temporally restricted signals. Because phosphatidylinositol 3-kinase (PI3K) plays an important role in the innate immune response, we studied the generation and distribution of 3′ phosphoinositides (3′PIs) in macrophages during the course of phagocytosis. The presence of 3′PI was monitored noninvasively in cells transfected with chimeras of green fluorescent protein and the pleckstrin homology domain of either Akt, Btk, or Gab1. Although virtually undetectable in unstimulated cells, 3′PI rapidly accumulated at sites of phagocytosis. This accumulation was sharply restricted to the phagosomal cup, with little 3′PI detectable in the immediately adjacent areas of the plasmalemma. Measurements of fluorescence recovery after photobleaching were made to estimate the mobility of lipids in the cytosolic monolayer of the phagosomal membrane. Stimulation of phagocytic receptors induced a marked reduction of lipid mobility that likely contributes to the restricted distribution of 3′PI at the cup. 3′PI accumulation during phagocytosis was transient, terminating shortly after sealing of the phagosomal vacuole. Two factors contribute to the rapid disappearance of 3′PI: the dissociation of the type I PI3K from the phagosomal membrane and the persistent accumulation of phosphoinositide phosphatases.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.153.7.1369
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2001
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Putting G protein–coupled receptor-mediated activation of phospholipase C in the limelight
    Rockefeller University Press ; 2010
    In:  Journal of General Physiology Vol. 135, No. 2 ( 2010-02-01), p. 77-80
    Details
    In: Journal of General Physiology, Rockefeller University Press, Vol. 135, No. 2 ( 2010-02-01), p. 77-80
    Type of Medium: Online Resource
    ISSN: 1540-7748 , 0022-1295
    URL: Article
    DOI: 10.1085/jgp.200910396
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2010
    detail.hit.zdb_id: 1477246-2
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  • 8
    Online Resource
    Online Resource
    Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells
    Rockefeller University Press ; 2006
    In:  The Journal of Cell Biology Vol. 175, No. 3 ( 2006-11-06), p. 377-382
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 175, No. 3 ( 2006-11-06), p. 377-382
    Abstract: Rapamycin (rapa)-induced heterodimerization of the FRB domain of the mammalian target of rapa and FKBP12 was used to translocate a phosphoinositide 5-phosphatase (5-ptase) enzyme to the plasma membrane (PM) to evoke rapid changes in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) levels. Rapa-induced PM recruitment of a truncated type IV 5-ptase containing only the 5-ptase domain fused to FKBP12 rapidly decreased PM PtdIns(4,5)P2 as monitored by the PLCδ1PH-GFP fusion construct. This decrease was paralleled by rapid termination of the ATP-induced Ca2+ signal and the prompt inactivation of menthol-activated transient receptor potential melastatin 8 (TRPM8) channels. Depletion of PM PtdIns(4,5)P2 was associated with a complete blockade of transferrin uptake and inhibition of epidermal growth factor internalization. None of these changes were observed upon rapa-induced translocation of an mRFP-FKBP12 fusion protein that was used as a control. These data demonstrate that rapid inducible depletion of PM PtdIns(4,5)P2 is a powerful tool to study the multiple regulatory roles of this phospholipid and to study differential sensitivities of various processes to PtdIns(4,5)P2 depletion.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200607116
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2006
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Dual roles for the Drosophila PI 4-kinase Four wheel drive in localizing Rab11 during cytokinesis
    Rockefeller University Press ; 2009
    In:  Journal of Cell Biology Vol. 187, No. 6 ( 2009-12-14), p. 847-858
    Details
    In: Journal of Cell Biology, Rockefeller University Press, Vol. 187, No. 6 ( 2009-12-14), p. 847-858
    Abstract: Successful completion of cytokinesis relies on addition of new membrane, and requires the recycling endosome regulator Rab11, which localizes to the midzone. Despite the critical role of Rab11 in this process, little is known about the formation and composition of Rab11-containing organelles. Here, we identify the phosphatidylinositol (PI) 4-kinase III β Four wheel drive (Fwd) as a key regulator of Rab11 during cytokinesis in Drosophila melanogaster spermatocytes. We show Fwd is required for synthesis of PI 4-phosphate (PI4P) on Golgi membranes and for formation of PI4P-containing secretory organelles that localize to the midzone. Fwd binds and colocalizes with Rab11 on Golgi membranes, and is required for localization of Rab11 in dividing cells. A kinase-dead version of Fwd also binds Rab11 and partially restores cytokinesis to fwd mutant flies. Moreover, activated Rab11 partially suppresses loss of fwd. Our data suggest Fwd plays catalytic and noncatalytic roles in regulating Rab11 during cytokinesis.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200908107
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2009
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
    Rockefeller University Press ; 2014
    In:  Journal of Cell Biology Vol. 205, No. 1 ( 2014-04-14), p. 113-126
    Details
    In: Journal of Cell Biology, Rockefeller University Press, Vol. 205, No. 1 ( 2014-04-14), p. 113-126
    Abstract: Polyphosphoinositides are an important class of lipid that recruit specific effector proteins to organelle membranes. One member, phosphatidylinositol 4-phosphate (PtdIns4P) has been localized to Golgi membranes based on the distribution of lipid binding modules from PtdIns4P effector proteins. However, these probes may be biased by additional interactions with other Golgi-specific determinants. In this paper, we derive a new PtdIns4P biosensor using the PtdIns4P binding of SidM (P4M) domain of the secreted effector protein SidM from the bacterial pathogen Legionella pneumophila. PtdIns4P was necessary and sufficient for localization of P4M, which revealed pools of the lipid associated not only with the Golgi but also with the plasma membrane and Rab7-positive late endosomes/lysosomes. PtdIns4P distribution was determined by the localization and activities of both its anabolic and catabolic enzymes. Therefore, P4M reports a wider cellular distribution of PtdIns4P than previous probes and therefore will be valuable for dissecting the biological functions of PtdIns4P in its assorted membrane compartments.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    URL: Article
    DOI: 10.1083/jcb.201312072
    DOI: 10.1083/jcb.201312072.dv
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2014
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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