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  1. Article ; Online: Macropinocytosis: mechanisms and regulation.

    Salloum, Gilbert / Bresnick, Anne R / Backer, Jonathan M

    The Biochemical journal

    2023  Volume 480, Issue 5, Page(s) 335–362

    Abstract: Macropinocytosis is defined as an actin-dependent but coat- and dynamin-independent endocytic uptake process, which generates large intracellular vesicles (macropinosomes) containing a non-selective sampling of extracellular fluid. Macropinocytosis ... ...

    Abstract Macropinocytosis is defined as an actin-dependent but coat- and dynamin-independent endocytic uptake process, which generates large intracellular vesicles (macropinosomes) containing a non-selective sampling of extracellular fluid. Macropinocytosis provides an important mechanism of immune surveillance by dendritic cells and macrophages, but also serves as an essential nutrient uptake pathway for unicellular organisms and tumor cells. This review examines the cell biological mechanisms that drive macropinocytosis, as well as the complex signaling pathways - GTPases, lipid and protein kinases and phosphatases, and actin regulatory proteins - that regulate macropinosome formation, internalization, and disposition.
    MeSH term(s) Actins ; Pinocytosis ; Endocytosis ; Signal Transduction ; Macrophages
    Chemical Substances Actins
    Language English
    Publishing date 2023-03-15
    Publishing country England
    Document type Review ; Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20210584
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  2. Article ; Online: The intricate regulation and complex functions of the Class III phosphoinositide 3-kinase Vps34.

    Backer, Jonathan M

    The Biochemical journal

    2016  Volume 473, Issue 15, Page(s) 2251–2271

    Abstract: The Class III phosphoinositide 3-kinase Vps34 (vacuolar protein sorting 34) plays important roles in endocytic trafficking, macroautophagy, phagocytosis, cytokinesis and nutrient sensing. Recent studies have provided exciting new insights into the ... ...

    Abstract The Class III phosphoinositide 3-kinase Vps34 (vacuolar protein sorting 34) plays important roles in endocytic trafficking, macroautophagy, phagocytosis, cytokinesis and nutrient sensing. Recent studies have provided exciting new insights into the structure and regulation of this lipid kinase, and new cellular functions for Vps34 have emerged. This review critically examines the wealth of new data on this important enzyme, and attempts to integrate these findings with current models of Vps34 signalling.
    MeSH term(s) Animals ; Autophagy ; Class III Phosphatidylinositol 3-Kinases/chemistry ; Class III Phosphatidylinositol 3-Kinases/metabolism ; Endosomes/enzymology ; Humans ; Phosphorylation ; Protein Conformation
    Chemical Substances Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137)
    Language English
    Publishing date 2016-08-01
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160170
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: PI3Kβ-A Versatile Transducer for GPCR, RTK, and Small GTPase Signaling.

    Bresnick, Anne R / Backer, Jonathan M

    Endocrinology

    2019  Volume 160, Issue 3, Page(s) 536–555

    Abstract: The phosphoinositide 3-kinase (PI3K) family includes eight distinct catalytic subunits and seven regulatory subunits. Only two PI3Ks are directly regulated downstream from G protein-coupled receptors (GPCRs): the class I enzymes PI3Kβ and PI3Kγ. Both ... ...

    Abstract The phosphoinositide 3-kinase (PI3K) family includes eight distinct catalytic subunits and seven regulatory subunits. Only two PI3Ks are directly regulated downstream from G protein-coupled receptors (GPCRs): the class I enzymes PI3Kβ and PI3Kγ. Both enzymes produce phosphatidylinositol 3,4,5-trisposphate in vivo and are regulated by both heterotrimeric G proteins and small GTPases from the Ras or Rho families. However, PI3Kβ is also regulated by direct interactions with receptor tyrosine kinases (RTKs) and their tyrosine phosphorylated substrates, and similar to the class II and III PI3Ks, it binds activated Rab5. The unusually complex regulation of PI3Kβ by small and trimeric G proteins and RTKs leads to a rich landscape of signaling responses at the cellular and organismic levels. This review focuses first on the regulation of PI3Kβ activity in vitro and in cells, and then summarizes the biology of PI3Kβ signaling in distinct tissues and in human disease.
    MeSH term(s) Animals ; Class Ia Phosphatidylinositol 3-Kinase/chemistry ; Class Ia Phosphatidylinositol 3-Kinase/genetics ; Class Ia Phosphatidylinositol 3-Kinase/metabolism ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; Humans ; Molecular Structure ; Mutation ; Neoplasms/genetics ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
    Chemical Substances Receptors, G-Protein-Coupled ; Class Ia Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; GTP Phosphohydrolases (EC 3.6.1.-)
    Language English
    Publishing date 2019-01-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 427856-2
    ISSN 1945-7170 ; 0013-7227
    ISSN (online) 1945-7170
    ISSN 0013-7227
    DOI 10.1210/en.2018-00843
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: PIP

    Jakubik, Charles T / Weckerly, Claire C / Hammond, Gerald R V / Bresnick, Anne R / Backer, Jonathan M

    FEBS letters

    2022  Volume 596, Issue 4, Page(s) 417–426

    Abstract: PI3Kβ is required for invadopodia-mediated matrix degradation by breast cancer cells. Invadopodia maturation requires GPCR activation of PI3Kβ and its coupling to SHIP2 to produce PI(3,4) ... ...

    Abstract PI3Kβ is required for invadopodia-mediated matrix degradation by breast cancer cells. Invadopodia maturation requires GPCR activation of PI3Kβ and its coupling to SHIP2 to produce PI(3,4)P
    MeSH term(s) Cell Line, Tumor ; Cell Movement ; Class I Phosphatidylinositol 3-Kinases/genetics ; Class I Phosphatidylinositol 3-Kinases/metabolism ; Diglycerides/chemistry ; Extracellular Matrix/metabolism ; Extracellular Matrix/ultrastructure ; Female ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Mammary Glands, Human/cytology ; Mammary Glands, Human/metabolism ; Mutation ; Phosphatidylinositol Phosphates/metabolism ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases/genetics ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases/metabolism ; Podosomes/metabolism ; Podosomes/ultrastructure ; Signal Transduction
    Chemical Substances Diglycerides ; Phosphatidylinositol Phosphates ; 1,2-dioctanoylglycerol (1069-87-0) ; Class I Phosphatidylinositol 3-Kinases (EC 2.7.1.137) ; PIK3CA protein, human (EC 2.7.1.137) ; PIK3CB protein, human (EC 2.7.1.137) ; INPPL1 protein, human (EC 3.1.3.86) ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases (EC 3.1.3.86)
    Language English
    Publishing date 2022-01-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14273
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: PIP3 abundance overcomes PI3K signaling selectivity in invadopodia

    Jakubik, Charles T. / Weckerly, Claire C. / Hammond, Gerald R.V. / Bresnick, Anne R. / Backer, Jonathan M.

    FEBS letters. 2022 Feb., v. 596, no. 4

    2022  

    Abstract: PI3Kβ is required for invadopodia‐mediated matrix degradation by breast cancer cells. Invadopodia maturation requires GPCR activation of PI3Kβ and its coupling to SHIP2 to produce PI(3,4)P₂. We now test whether selectivity for PI3Kβ is preserved under ... ...

    Abstract PI3Kβ is required for invadopodia‐mediated matrix degradation by breast cancer cells. Invadopodia maturation requires GPCR activation of PI3Kβ and its coupling to SHIP2 to produce PI(3,4)P₂. We now test whether selectivity for PI3Kβ is preserved under conditions of mutational increases in PI3K activity. In breast cancer cells where PI3Kβ is inhibited, short‐chain diC8‐PIP₃ rescues gelatin degradation in a SHIP2‐dependent manner; rescue by diC8‐PI(3,4)P₂ is SHIP2‐independent. Surprisingly, the expression of either activated PI3Kβ or PI3Kα mutants rescued the effects of PI3Kβ inhibition. In both cases, gelatin degradation was SHIP2‐dependent. These data confirm the requirement for PIP₃ conversion to PI(3,4)P₂ for invadopodia function and suggest that selectivity for distinct PI3K isotypes may be obviated by mutational activation of the PI3K pathway.
    Keywords breast neoplasms ; gelatin ; phosphatidylinositol 3-kinase
    Language English
    Dates of publication 2022-02
    Size p. 417-426.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14273
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  6. Article: The regulation of class IA PI 3-kinases by inter-subunit interactions.

    Backer, Jonathan M

    Current topics in microbiology and immunology

    2010  Volume 346, Page(s) 87–114

    Abstract: Phosphoinositide 3-kinases (PI 3-kinases) are activated by growth factor and hormone receptors, and regulate cell growth, survival, motility, and responses to changes in nutritional conditions (Engelman et al. 2006). PI 3-kinases have been classified ... ...

    Abstract Phosphoinositide 3-kinases (PI 3-kinases) are activated by growth factor and hormone receptors, and regulate cell growth, survival, motility, and responses to changes in nutritional conditions (Engelman et al. 2006). PI 3-kinases have been classified according to their subunit composition and their substrate specificity for phosphoinositides (Vanhaesebroeck et al. 2001). The class IA PI 3-kinase is a heterodimer consisting of one regulatory subunit (p85α, p85β, p55α, p50α, or p55γ) and one 110-kDa catalytic subunit (p110α, β or δ). The Class IB PI 3-kinase is also a dimer, composed of one regulatory subunit (p101 or p87) and one catalytic subunit (p110γ) (Wymann et al. 2003). Class I enzymes will utilize PI, PI[4]P, or PI[4,5]P2 as substrates in vitro, but are thought to primarily produce PI[3,4,5]P3 in cells.The crystal structure of the Class IB PI 3-kinase catalytic subunit p110γ was solved in 1999 (Walker et al. 1999), and crystal or NMR structures of the Class IA p110α catalytic subunit and all of the individual domains of the Class IA p85α regulatory subunit have been solved (Booker et al. 1992; Günther et al. 1996; Hoedemaeker et al. 1999; Huang et al. 2007; Koyama et al. 1993; Miled et al. 2007; Musacchio et al. 1996; Nolte et al. 1996; Siegal et al. 1998). However, a structure of an intact PI 3-kinase enzyme has remained elusive. In spite of this, studies over the past 10 years have lead to important insights into how the enzyme is regulated under physiological conditions. This chapter will specifically discuss the regulation of Class IA PI 3-kinase enzymatic activity, focusing on regulatory interactions between the p85 and p110 subunits and the modulation of these interactions by physiological activators and oncogenic mutations. The complex web of signaling downstream from Class IA PI 3-kinases will be discussed in other chapters in this volume.
    MeSH term(s) Animals ; Enzyme Activation ; Humans ; Mutation ; Phosphatidylinositol 3-Kinases/chemistry ; Phosphatidylinositol 3-Kinases/physiology ; Phosphorylation ; Protein Structure, Tertiary ; Protein Subunits ; src Homology Domains
    Chemical Substances Protein Subunits ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2010-06-11
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0070-217X
    ISSN 0070-217X
    DOI 10.1007/82_2010_52
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  7. Article ; Online: New methods for capturing the mystery lipid, PtdIns5P.

    Backer, Jonathan M

    The Biochemical journal

    2010  Volume 428, Issue 3, Page(s) e1–2

    Abstract: The enormous versatility of phosphatidylinositol as a mediator of intracellular signalling is due to its variable phosphorylation on every combination of the 3', 4' and 5' positions, as well as an even more complex range of phosphorylated products when ... ...

    Abstract The enormous versatility of phosphatidylinositol as a mediator of intracellular signalling is due to its variable phosphorylation on every combination of the 3', 4' and 5' positions, as well as an even more complex range of phosphorylated products when inositol phosphate is released by phospholipase C activity. The phosphoinositides are produced by distinct enzymes in distinct intracellular membranes, and recruit and regulate downstream signalling proteins containing binding domains [PH (pleckstrin homology), PX (Phox homology), FYVE etc.] that are relatively specific for these lipids. Specific recruitment of downstream proteins presumably involves a coincidence detection mechanism, in which a combination of lipid-protein and protein-protein interactions define specificity. Of the seven intracellular phosphoinositide, quantification of PtdIns5P levels in intact cells has remained difficult. In this issue of the Biochemical Journal, Sarkes and Rameh describe a novel HPLC-based approach which makes possible an analysis of the subcellular distribution of PtdIns5P and other phosphoinositides.
    MeSH term(s) Binding Sites ; Chromatography, High Pressure Liquid ; Phosphatidylinositol Phosphates/analysis ; Phosphatidylinositol Phosphates/chemistry ; Phosphatidylinositol Phosphates/metabolism ; Signal Transduction
    Chemical Substances Phosphatidylinositol Phosphates ; phosphatidylinositol 5-phosphate
    Language English
    Publishing date 2010-05-27
    Publishing country England
    Document type Comment ; Journal Article
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BJ20100688
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: PI3Kβ links integrin activation and PI(3,4)P

    Erami, Zahra / Heitz, Samantha / Bresnick, Anne R / Backer, Jonathan M

    Molecular biology of the cell

    2019  Volume 30, Issue 18, Page(s) 2367–2376

    Abstract: The invasion of tumor cells from the primary tumor is mediated by invadopodia, actin-rich protrusive organelles that secrete matrix metalloproteases and degrade the extracellular matrix. This coupling between protrusive activity and matrix degradation ... ...

    Abstract The invasion of tumor cells from the primary tumor is mediated by invadopodia, actin-rich protrusive organelles that secrete matrix metalloproteases and degrade the extracellular matrix. This coupling between protrusive activity and matrix degradation facilitates tumor invasion. We previously reported that the PI3Kβ isoform of PI 3-kinase, which is regulated by both receptor tyrosine kinases and G protein-coupled receptors, is required for invasion and gelatin degradation in breast cancer cells. We have now defined the mechanism by which PI3Kβ regulates invadopodia. We find that PI3Kβ is specifically activated downstream from integrins, and is required for integrin-stimulated spreading and haptotaxis as well as integrin-stimulated invadopodia formation. Surprisingly, these integrin-stimulated and PI3Kβ-dependent responses require the production of PI(3,4)P
    MeSH term(s) Actins/metabolism ; Breast Neoplasms/metabolism ; Cell Line, Tumor ; Chemotaxis/physiology ; Extracellular Matrix/metabolism ; Female ; Humans ; Integrins/metabolism ; Integrins/physiology ; Neoplasm Invasiveness/pathology ; Phosphatidylinositol 3-Kinase/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols/metabolism ; Phosphorylation ; Podosomes/metabolism ; Podosomes/physiology ; Signal Transduction/physiology
    Chemical Substances Actins ; Integrins ; Phosphatidylinositols ; phosphoinositide-3,4-bisphosphate ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137)
    Language English
    Publishing date 2019-07-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E19-03-0182
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  9. Article ; Online: The regulation and function of Class III PI3Ks: novel roles for Vps34.

    Backer, Jonathan M

    The Biochemical journal

    2008  Volume 410, Issue 1, Page(s) 1–17

    Abstract: The Class III PI3K (phosphoinositide 3-kinase), Vps34 (vacuolar protein sorting 34), was first described as a component of the vacuolar sorting system in Saccharomyces cerevisiae and is the sole PI3K in yeast. The homologue in mammalian cells, hVps34, ... ...

    Abstract The Class III PI3K (phosphoinositide 3-kinase), Vps34 (vacuolar protein sorting 34), was first described as a component of the vacuolar sorting system in Saccharomyces cerevisiae and is the sole PI3K in yeast. The homologue in mammalian cells, hVps34, has been studied extensively in the context of endocytic sorting. However, hVps34 also plays an important role in the ability of cells to respond to changes in nutrient conditions. Recent studies have shown that mammalian hVps34 is required for the activation of the mTOR (mammalian target of rapamycin)/S6K1 (S6 kinase 1) pathway, which regulates protein synthesis in response to nutrient availability. In both yeast and mammalian cells, Class III PI3Ks are also required for the induction of autophagy during nutrient deprivation. Finally, mammalian hVps34 is itself regulated by nutrients. Thus Class III PI3Ks are implicated in the regulation of both autophagy and, through the mTOR pathway, protein synthesis, and thus contribute to the integration of cellular responses to changing nutritional status.
    MeSH term(s) Endocytosis ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Transport ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Saccharomyces cerevisiae Proteins ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2008-02-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BJ20071427
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Phosphatidylinositol-3,4,5-trisphosphate: tool of choice for class I PI 3-kinases.

    Salamon, Rachel Schnur / Backer, Jonathan M

    BioEssays : news and reviews in molecular, cellular and developmental biology

    2013  Volume 35, Issue 7, Page(s) 602–611

    Abstract: Class I PI 3-kinases signal by producing the signaling lipid phosphatidylinositol(3,4,5) trisphosphate, which in turn acts by recruiting downstream effectors that contain specific lipid-binding domains. The class I PI 3-kinases comprise four distinct ... ...

    Abstract Class I PI 3-kinases signal by producing the signaling lipid phosphatidylinositol(3,4,5) trisphosphate, which in turn acts by recruiting downstream effectors that contain specific lipid-binding domains. The class I PI 3-kinases comprise four distinct catalytic subunits linked to one of seven different regulatory subunits. All the class I PI 3-kinases produce the same signaling lipid, PIP3, and the different isoforms have overlapping expression patterns and are coupled to overlapping sets of upstream activators. Nonetheless, studies in cultured cells and in animals have demonstrated that the different isoforms are coupled to distinct ranges of downstream responses. This review focuses on the mechanisms by which the production of a common product, PIP3, can produce isoform-specific signaling by PI 3-kinases.
    MeSH term(s) Animals ; Class I Phosphatidylinositol 3-Kinases/genetics ; Class I Phosphatidylinositol 3-Kinases/metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Isoenzymes/metabolism ; Models, Animal ; Phosphatidylinositol Phosphates/metabolism ; Protein Interaction Domains and Motifs ; Signal Transduction
    Chemical Substances Isoenzymes ; Phosphatidylinositol Phosphates ; phosphatidylinositol 3,4,5-triphosphate ; Class I Phosphatidylinositol 3-Kinases (EC 2.7.1.137)
    Language English
    Publishing date 2013-08-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 50140-2
    ISSN 1521-1878 ; 0265-9247
    ISSN (online) 1521-1878
    ISSN 0265-9247
    DOI 10.1002/bies.201200176
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