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1. Full Text Molecularly Distinct Clathrin-Coated Pits Differentially Impact EGFR Fate and Signaling
by Pascolutti, Roberta and Algisi, Veronica and Conte, Alexia and Raimondi, Andrea and Pasham, Mithun and Upadhyayula, Srigokul and Gaudin, Raphael and Maritzen, Tanja and Barbieri, Elisa and Caldieri, Giusi and Tordonato, Chiara and Confalonieri, Stefano and Freddi, Stefano and Malabarba, Maria Grazia and Maspero, Elena and Polo, Simona and Tacchetti, Carlo and Haucke, Volker and Kirchhausen, Tom and Di Fiore, Pier Paolo and Sigismund, Sara
Cell Reports, ISSN 2211-1247, 06/2019, Volume 27, Issue 10, pp. 3049 - 3061.e6
Adaptor protein 2 (AP2) is a major constituent of clathrin-coated pits (CCPs). Whether it is essential for all forms of clathrin-mediated endocytosis (CME) in... 
AP2 | signaling | transcription | clathrin-coated pits | receptor degradation | endocytosis | recycling | EGFR | epsin | eps15 | endocytic adaptors | Life Sciences
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2. EGFR Trafficking in Physiology and Cancer
by Caldieri, Giusi and Malabarba, Maria Grazia and Di Fiore, Pier Paolo and Sigismund, Sara
Progress in molecular and subcellular biology, ISSN 0079-6484, 01/2018, Volume 57, pp. 235 - 272
Signaling from the epidermal growth factor receptor (EGFR) elicits multiple biological responses, including cell proliferation, migration, and survival.... 
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3. Full Text Reticulon 3-dependent ER-PM contact sites control EGFR nonclathrin endocytosis
by Caldieri, Giusi and Barbieri, Elisa and Nappo, Gilda and Raimondi, Andrea and Bonora, Massimo and Conte, Alexia and Verhoef, Lisette G. G. C and Confalonieri, Stefano and Malabarba, Maria Grazia and Bianchi, Fabrizio and Cuomo, Alessandro and Bonaldi, Tiziana and Martini, Emanuele and Mazza, Davide and Pinton, Paolo and Tacchetti, Carlo and Polo, Simona and Di Fiore, Pier Paolo and Sigismund, Sara
Science, ISSN 0036-8075, 05/2017, Volume 356, Issue 6338, pp. 617 - 624
The integration of endocytic routes is critical to regulate receptor signaling. A nonclathrin endocytic (NCE) pathway of the epidermal growth factor receptor... 
CELLS | ENDOSOMES | INTERNALIZATION | CLATHRIN-INDEPENDENT ENDOCYTOSIS | PATHWAY | MULTIDISCIPLINARY SCIENCES | TUBULAR ENDOPLASMIC-RETICULUM | PROTEINS | PLASMA-MEMBRANE | EXPRESSION | PITS | Nerve Tissue Proteins - metabolism | Cell Line | Endocytosis | Carrier Proteins - metabolism | ErbB Receptors - metabolism | Humans | Basigin - metabolism | Endoplasmic Reticulum - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Calcium Signaling | Physiological aspects | Observations | Endoplasmic reticulum | Invaginations | Clathrin | Calcium channels | Integration | Epidermal growth factor receptors | Cortex | CD147 antigen | Intermediates | Degradation | Calcium signalling | Inositols | Signal transduction | Epidermal growth factor | Internalization | Ligands | Molecular biology | Inositol 1,4,5-trisphosphate | Inositol 1,4,5-trisphosphate receptors | Cargo | Regulators | Receptors | Maturation | Pathways | Formations | Contact
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4. A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer
by Ivan Nicola Colaluca and Andrea Basile and Lee Freiburger and Veronica D'Uva and Davide Disalvatore and Manuela Vecchi and Stefano Confalonieri and Daniela Tosoni and Valentina Cecatiello and Maria Grazia Malabarba and Chun-Jiun Yang and Masatsune Kainosho and Michael Sattler and Marina Mapelli and Salvatore Pece and Pier Paolo Di Fiore
The Journal of Cell Biology, ISSN 0021-9525, 02/2018, Volume 217, Issue 2, p. 745
Numb functions as an oncosuppressor by inhibiting Notch signaling and stabilizing p53. This latter effect depends on the interaction of Numb with Mdm2, the E3... 
Alternative splicing | MDM2 protein | Splicing | Toxicity | p53 Protein | Genotoxicity | Chemoresistance | Homeostasis | Breast cancer | Fuzzy logic | Degradation | Signaling | Stem cells | Isoforms | NUMB protein | Notch protein | Ubiquitin-protein ligase | Tumors | Cancer
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5. Full Text A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer
by Colaluca, IN and Basile, A and Freiburger, L and D'Uva, V and Disalvatore, D and Vecchi, M and Confalonieri, S and Tosoni, D and Cecatiello, V and Malabarba, MG and Yang, CJ and Kainosho, M and Sattler, M and Mapelli, M and Pece, S and Di Fiore, PP
JOURNAL OF CELL BIOLOGY, ISSN 0021-9525, 02/2018, Volume 217, Issue 2, pp. 745 - 762
Numb functions as an oncosuppressor by inhibiting Notch signaling and stabilizing p53. This latter effect depends on the interaction of Numb with Mdm2, the E3... 
MAMMALIAN NUMB | PROTEIN | UBIQUITIN LIGASE | PROMOTES NEURONAL DIFFERENTIATION | NMR EXPERIMENTS | MDM2 | DEGRADATION | HISTONE H2AX | P53 PATHWAY | CELL FATE | CELL BIOLOGY | Proto-Oncogene Proteins c-mdm2 - genetics | Alternative Splicing | Membrane Proteins - genetics | Humans | Tumor Suppressor Protein p53 - metabolism | Nerve Tissue Proteins - genetics | Breast Neoplasms - metabolism | Nerve Tissue Proteins - metabolism | Protein Isoforms - metabolism | Breast Neoplasms - pathology | Cell Line, Tumor | Female | Membrane Proteins - metabolism | Proto-Oncogene Proteins c-mdm2 - metabolism | Protein Isoforms - genetics
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6. Full Text Epithelial-to-mesenchymal plasticity harnesses endocytic circuitries
by Corallino, Salvatore and Malabarba, Maria Grazia and Zobel, Martina and Di Fiore, Pier Paolo and Scita, Giorgio
Frontiers in Oncology, ISSN 2234-943X, 2015, Volume 5, p. 45
The ability of cells to alter their phenotypic and morphological characteristics, known as cellular plasticity, is critical in normal embryonic development and... 
FYVE DOMAIN PROTEIN | GLYCOGEN-SYNTHASE KINASE-3 | endocytic pathway | E-CADHERIN ENDOCYTOSIS | AMYLOID PRECURSOR PROTEIN | endocytosis and EMT | CANCER STEM-CELLS | SMAD ANCHOR | ONCOLOGY | epithelial junctions remodeling | WNT and TGF-beta signaling | TGF-BETA RECEPTOR | ADHERENS JUNCTIONS | CELL-CELL ADHESION | SENSORY ORGAN PRECURSOR | EMT and cancer | WNT and TGFBeta signalling | Epithelial junctions remodelling
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7. Full Text Interleukin 4 regulates phosphorylation of serine 756 in the transactivation domain of stat6: Roles for multiple phosphorylation sites and stat6 function
by Wang, Yuling and Malabarba, Maria Grazia and Nagy, Zsuzsanna S and Kirken, Robert A
Journal of Biological Chemistry, ISSN 0021-9258, 06/2004, Volume 279, Issue 24, pp. 25196 - 25203
Lymphokines interleukin-4 (IL4) and IL13 exert overlapping biological activities via the shared use of the IL4 receptor alpha-chain and signal transducer and... 
TYROSINE-PHOSPHATASE SHP-1 | SIGNAL-TRANSDUCTION | CYTOPLASMIC DOMAIN | TRANSCRIPTIONAL ACTIVATION | GLUCOCORTICOID-RECEPTOR | HUMAN IL-4 RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-EXPRESSION | MAXIMAL ACTIVATION | NF-KAPPA-B | T-LYMPHOCYTES | Amino Acid Sequence | Phosphorylation | Humans | Transcriptional Activation | Molecular Sequence Data | Structure-Activity Relationship | DNA - metabolism | Interleukin-13 - pharmacology | Phosphoprotein Phosphatases - physiology | Trans-Activators - chemistry | Serine - metabolism | STAT6 Transcription Factor | Trans-Activators - physiology | Interleukin-4 - pharmacology | Tyrosine - metabolism | T-Lymphocytes - metabolism | Phytohemagglutinins - pharmacology | Protein Phosphatase 2
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8. Full Text A Numb-Mdm2 fuzzy complex reveals an isoformspecific involvement of Numb in breast cancer
by Colaluca, Ivan Nicola and Basile, Andrea and Freiburger, Lee and D'Uva, Veronica and Disalvatore, Davide and Vecchi, Manuela and Confalonieri, Stefano and Tosoni, Daniela and Cecatiello, Valentina and Malabarba, Maria Grazia and Yang, Chun-Jiun and Kainosho, Masatsune and Sattler, Michael and Mapelli, Marina and Pece, Salvatore and di Fiore, Pier Paolo
Journal of Cell Biology, ISSN 0021-9525, 02/2018, Volume 217, Issue 2, pp. 745 - 762
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9. Full Text The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5
by Lanzetti, Letizia and Rybin, Vladimir and Malabarba, Maria Grazia and Christoforidis, Savvas and Scita, Giorgio and Zerial, Marino and Di Fiore, Pier Paolo
Nature, ISSN 0028-0836, 11/2000, Volume 408, Issue 6810, pp. 374 - 377
How epidermal growth factor receptor (EGFR) signalling is linked to EGFR trafficking is largely unknown. Signalling and trafficking involve small GTPases of... 
FUSION | ENDOCYTIC PATHWAY | GTPASE-ACTIVATING PROTEINS | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | GROWTH | KINASE | BINDING-PROTEIN | E3B1 | SH3 DOMAIN | Cytoskeletal Proteins | Protein Structure, Tertiary | Proteins - physiology | Oncogene Proteins, Fusion - metabolism | GTPase-Activating Proteins | Signal Transduction | Humans | SOS1 Protein - metabolism | Intracellular Signaling Peptides and Proteins | rac GTP-Binding Proteins - metabolism | rab5 GTP-Binding Proteins - metabolism | Recombinant Fusion Proteins | Adaptor Proteins, Signal Transducing | Endocytosis | Receptor, Epidermal Growth Factor - metabolism | Animals | Carrier Proteins - metabolism | Cloning, Molecular | Protein Binding | Catalysis | HeLa Cells | COS Cells | Proteins | Cellular biology | Mutation
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10. Full Text Reticulon3-dependent ER-PM contact sites control EGFR non-clathrin endocytosis
by Caldieri, Giusi and Barbieri, Elisa and Nappo, Gilda and Raimondi, Andrea and Bonora, Massimo and Conte, Alexia and Verhoef, Lisette G.G.C and Confalonieri, Stefano and Malabarba, Maria Grazia and Bianchi, Fabrizio and Cuomo, Alessandro and Bonaldi, Tiziana and Martini, Emanuele and Mazza, Davide and Pinton, Paolo and Tacchetti, Carlo and Polo, Simona and Di Fiore, Pier Paolo and Sigismund, Sara
Science (New York, N.Y.), ISSN 0036-8075, 5/2017, Volume 356, Issue 6338, pp. 617 - 624
The integration of endocytic routes is critical to regulate receptor signaling. A non-clathrin endocytic pathway (NCE) of the epidermal growth factor receptor... 
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11. Full Text Molecular basis for the dual function of Eps8 on actin dynamics: Bundling and capping
by Hertzog, Maud and Milanesi, Francesca and Hazelwood, Larnele and Disanza, Andrea and Liu, Hongjun and Perlade, Emilie and Malabarba, Maria Grazia and Pasqualato, Sebastiano and Maiolica, Alessio and Confalonieri, Stefano and Le Clainche, Christophe and Offenhauser, Nina and Block, Jennifer and Rottner, Klemens and Fiore, Pier Paolo Di and Carlier, Marie-France and Volkmann, Niels and Hanein, Dorit and Scita, Giorgio
PLoS Biology, ISSN 1544-9173, 06/2010, Volume 8, Issue 6, p. e1000387
Actin capping and cross-linking proteins regulate the dynamics and architectures of different cellular protrusions. Eps8 is the founding member of a unique... 
F-ACTIN | FILAMENT BARBED END | INSULIN-RECEPTOR | CAENORHABDITIS-ELEGANS | HOMOLOGY DOMAIN | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOLOGY | ELECTRON-MICROSCOPY | INTERTWINED DIMER | SH3 DOMAIN | Thermodynamics | Adaptor Proteins, Signal Transducing | Humans | Mass Spectrometry | Actins - metabolism | Models, Molecular | Protein Binding | Intracellular Signaling Peptides and Proteins - metabolism | Intracellular Signaling Peptides and Proteins - physiology | Microscopy, Electron | Actins - physiology | Proteins | Medical research | Motility | Cellular biology | Microscopy | Cytoskeleton | Grants | Experiments | Cell adhesion & migration
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12. Full Text A repertoire library that allows the selection of synthetic SH2ITALT with altered binding specificities
by Malabarba, Maria Grazia and Milia, Elisabetta and Faretta, Mario and Zamponi, Raffaella and Pelicci, Pier Giuseppe and Di Fiore, Pier Paolo
Oncogene, ISSN 0950-9232, 08/2001, Volume 20, Issue 37, pp. 5186 - 5194
Phosphotyrosine | Scaffold library | Scaffold | SH2
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13. Full Text Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and membrane trafficking during Caenorhabditis elegans oocyte growth and embryonic epidermal morphogenesis
by Giuliani, Chiara and Troglio, Flavia and Bai, Zhiyong and Patel, Falshruti B and Zucconi, Adriana and Malabarba, Maria Grazia and Disanza, Andrea and Stradal, Theresia B and Cassata, Giuseppe and Confalonieri, Stefano and Hardin, Jeffrey D and Soto, Martha C and Grant, Barth D and Scita, Giorgio
PLoS Genetics, ISSN 1553-7390, 10/2009, Volume 5, Issue 10, pp. e1000675 - e1000675
The TOCA family of F-BAR-containing proteins bind to and remodel lipid bilayers via their conserved F-BAR domains, and regulate actin dynamics via their N-Wasp... 
CLATHRIN-MEDIATED ENDOCYTOSIS | EPITHELIAL-CELLS | STRUCTURAL BASIS | GENETICS & HEREDITY | WASP-WIP COMPLEX | C-ELEGANS | N-WASP | ADHERENS JUNCTIONS | ALDRICH-SYNDROME PROTEIN | TIGHT JUNCTION | MISSING-IN-METASTASIS | Epidermis - metabolism | Caenorhabditis elegans - metabolism | Oocytes - growth & development | Caenorhabditis elegans - growth & development | Caenorhabditis elegans - genetics | Membrane Proteins - genetics | Oocytes - metabolism | Actins - metabolism | Caenorhabditis elegans Proteins - metabolism | Male | Cell Membrane - genetics | Caenorhabditis elegans - embryology | Epidermis - growth & development | Protein Transport | Morphogenesis | Animals | Epidermis - embryology | Protein Binding | Female | Cell Membrane - metabolism | Membrane Proteins - metabolism | Caenorhabditis elegans Proteins - genetics | Physiological aspects | Embryonic development | Genetic aspects | Research | Actin | Membrane proteins | Proteins | Medical research | Plasma | Motility | Cellular biology | Cytoskeleton | Experiments | Cell adhesion & migration
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14. Full Text A novel actin barbed-end-capping activity in EPS-8 regulates apical morphogenesis in intestinal cells of Caenorhabditis elegans
by Baumeister, Ralf and Disanza, Andrea and Malabarba, Maria Grazia and Carlier, Marie-France and Croce, Assunta and Cassata, Giuseppe and Gagliani, Maria Cristina and Tacchetti, Carlo and Fiore, Pier Paolo Di and Scita, Giorgio
Nature Cell Biology, ISSN 1465-7392, 12/2004, Volume 6, Issue 12, pp. 1173 - 1179
Redundant gene function frequently hampers investigations of the physiological roles of mammalian proteins. This is the case for Eps8, a receptor tyrosine... 
ORGANIZATION | ACTIVATION | COMPLEX | BUNDLES | RAC | SIGNALS | PROTEINS | SOS-1 | EPS15 | FAMILY | CELL BIOLOGY | Cytoskeletal Proteins | Epithelial Cells - metabolism | DNA, Complementary - genetics | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Intestines - embryology | Intestines - metabolism | Protein Isoforms - metabolism | DNA, Complementary - analysis | Microscopy, Electron, Transmission | Actin Cytoskeleton - metabolism | Actins - biosynthesis | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - genetics | Epithelial Cells - ultrastructure | Caenorhabditis elegans Proteins - isolation & purification | Protein Structure, Tertiary - genetics | Caenorhabditis elegans - embryology | Sequence Homology, Nucleic Acid | Intestines - ultrastructure | Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing | Animals | Carrier Proteins - metabolism | Microvilli - metabolism | Microvilli - ultrastructure | Carrier Proteins - isolation & purification | Organogenesis - physiology | Actin Cytoskeleton - ultrastructure | Caenorhabditis elegans Proteins - genetics | Protein Isoforms - genetics | Morphogenesis | Physiological aspects | Caenorhabditis elegans | Genetic aspects | Research | Actin
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15. Full Text A Snapshot of the Physical and Functional Wiring of the Eps15 Homology Domain Network in the Nematode
by Tsushima, Hanako and Malabarba, Maria Grazia and Confalonieri, Stefano and Senic-Matuglia, Francesca and Verhoef, Lisette G. G. C and Bartocci, Cristina and D'Ario, Giovanni and Cocito, Andrea and Di Fiore, Pier Paolo and Salcini, Anna Elisabetta
PLoS ONE, ISSN 1932-6203, 02/2013, Volume 8, Issue 2, p. e56383
Protein interaction modules coordinate the connections within and the activity of intracellular signaling networks. The Eps15 Homology (EH) module, a... 
CAENORHABDITIS-ELEGANS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | BINDING DOMAIN | ENDOCYTIC PROTEINS | C-ELEGANS | AMYLOID PRECURSOR PROTEIN | EH-DOMAIN | FAMILY PROTEINS | TYROSINE KINASE SUBSTRATE | ADAPTER PROTEIN | Protein Structure, Tertiary | Two-Hybrid System Techniques | Reproducibility of Results | Animals | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - genetics | Caenorhabditis elegans Proteins - chemistry | Gene Expression Regulation | Caenorhabditis elegans Proteins - metabolism | Adaptor Proteins, Vesicular Transport - chemistry | Adaptor Proteins, Vesicular Transport - metabolism | Synaptic Transmission | Physiological aspects | Cellular signal transduction | Muscle proteins | Nematoda | Space shuttles | Protein-protein interactions | Neurosciences | Peptides | Trafficking | Genes | Homology | Intracellular signalling | Genomes | DNA repair | Protein turnover | Proteins | Wiring | Signal transduction | Endocytosis | Ubiquitination | Actin | Physiology | Repair | Deoxyribonucleic acid--DNA | MiRNA | Metabolism | Mammals | DNA biosynthesis | MicroRNAs | Nematodes | Transduction | Alzheimers disease | Protein interaction | Neurotransmission | Deoxyribonucleic acid | DNA
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