The Experts below are selected from a list of 321 Experts worldwide ranked by ideXlab platform

Eugenio Monti - One of the best experts on this subject based on the ideXlab platform.

  • Sialidase NEU3 is a Peripheral Membrane Protein localized on the cell surface and in endosomal structures.
    Biochemical Journal, 2007
    Co-Authors: Gabriele Zanchetti, Paolo Colombi, Marta Manzoni, Luigi Anastasia, Luigi Caimi, Giuseppe Borsani, Bruno Venerando, Guido Tettamanti, Augusto Preti, Eugenio Monti
    Abstract:

    Sialidase NEU3 is also known as the plasma-Membrane-associated form of mammalian sialidases, exhibiting a high substrate specificity towards gangliosides. In this respect, sialidase NEU3 modulates cell-surface biological events and plays a pivotal role in different cellular processes, including cell adhesion, recognition and differentiation. At the moment, no detailed studies concerning the subcellular localization of NEU3 are available, and the mechanism of its association with cellular Membranes is still unknown. In the present study, we have demonstrated that sialidase NEU3, besides its localization at the plasma Membrane, is present in intracellular structures at least partially represented by a subset of the endosomal compartment. Moreover, we have shown that NEU3 present at the plasma Membrane is internalized and locates then to the recycling endosomal compartment. The enzyme is associated with the outer leaflet of the plasma Membrane, as shown by selective cell-surface Protein biotinylation. This evidence is in agreement with the ability of NEU3 to degrade gangliosides inserted into the plasma Membrane of adjacent cells. Moreover, the mechanism of the Protein association with the lipid bilayer was elucidated by carbonate extraction. Under these experimental conditions, we have succeeded in solubilizing NEU3, thus demonstrating that the enzyme is a Peripheral Membrane Protein. In addition, Triton X-114 phase separation demonstrates further the hydrophilic nature of the Protein. Overall, these results provide important information about the biology of NEU3, the most studied member of the mammalian sialidase family.

  • Sialidase NEU3 is a Peripheral Membrane Protein localized on the cell surface and in endosomal structures
    Biochemical Journal, 2007
    Co-Authors: Gabriele Zanchetti, Paolo Colombi, Marta Manzoni, Luigi Anastasia, Luigi Caimi, Giuseppe Borsani, Bruno Venerando, Guido Tettamanti, Augusto Preti, Eugenio Monti
    Abstract:

    Sialidase NEU3 is also known as the plasma Membrane-associated form of mammalian sialidases, exhibiting a high substrate specificity toward gangliosides. In this respect, sialidase NEU3 modulates cell surface biological events and plays a pivotal role in different cellular processes, including cell adhesion, recognition and differentiation. At the moment, no detailed studies concerning the subcellular localization of NEU3 are available and the mechanism of its association to cellular Membranes is still unknown. Here we demonstrate that sialidase NEU3, besides its localization at the plasma Membrane, is present in intracellular structures at least partially represented by a subset of the endosomal compartment. Moreover, we show that NEU3 present at the plasma Membrane is internalized and locates then to the recycling endosomal compartment. The enzyme is associated to the outer leaflet of the plasma Membrane, as shown by selective cell surface Protein biotinylation. This evidence is in agreement with the ability of NEU3 in degrading gangliosides inserted in the plasma Membrane of adjacent cells. Moreover, the association mechanism of the Protein to the lipid bilayer was elucidated by carbonate extraction. Under these experimental conditions we succeeded in solubilizing NEU3, thus demonstrating that the enzyme is a Peripheral Membrane Protein. In addition, Triton X-114 phase separation further demonstrates the hydrophilic nature of the Protein. Overall, these results provide important information about the biology of NEU3, the most studied member of the mammalian sialidase family.

Henry R. Bourne - One of the best experts on this subject based on the ideXlab platform.

  • Localization of a Peripheral Membrane Protein: Gβγ targets GαZ
    Proceedings of the National Academy of Sciences of the United States of America, 2000
    Co-Authors: C. Simone Fishburn, Sonia K. Pollitt, Henry R. Bourne
    Abstract:

    To explore the relative roles of Protein-binding partners vs. lipid modifications in controlling Membrane targeting of a typical Peripheral Membrane Protein, Gαz, we directed its binding partner, βγ, to mislocalize on mitochondria. Mislocalized βγ directed wild-type Gαz and a palmitate-lacking Gαz mutant to mitochondria but did not alter localization of a Gαz mutant lacking both myristate and palmitate. Thus, in this paradigm, a Protein–Protein interaction controls targeting of a Peripheral Membrane Protein to the proper compartment, whereas lipid modifications stabilize interactions of Proteins with Membranes and with other Proteins.

  • Localization of a Peripheral Membrane Protein: Gβγ targets GαZ
    Proceedings of the National Academy of Sciences of the United States of America, 2000
    Co-Authors: C. Simone Fishburn, Sonia K. Pollitt, Henry R. Bourne
    Abstract:

    To explore the relative roles of Protein-binding partners vs. lipid modifications in controlling Membrane targeting of a typical Peripheral Membrane Protein, Galpha(z), we directed its binding partner, betagamma, to mislocalize on mitochondria. Mislocalized betagamma directed wild-type Galpha(z) and a palmitate-lacking Galpha(z) mutant to mitochondria but did not alter localization of a Galpha(z) mutant lacking both myristate and palmitate. Thus, in this paradigm, a Protein-Protein interaction controls targeting of a Peripheral Membrane Protein to the proper compartment, whereas lipid modifications stabilize interactions of Proteins with Membranes and with other Proteins.

Jean Gruenberg - One of the best experts on this subject based on the ideXlab platform.

  • the p11 s100a10 light chain of annexin a2 is dispensable for annexin a2 association to endosomes and functions in endosomal transport
    PLOS ONE, 2007
    Co-Authors: Etienne Morel, Jean Gruenberg
    Abstract:

    Annexin A2 is a Peripheral Membrane Protein that belongs to the annexin family of Ca2+ and phospholipid-binding Proteins. This Protein, which plays a role in Membrane organization and dynamics in particular along the endocytic pathway, exists as a heterotetrameric complex, consisting of two annexin A2 molecules bound via their N-termini to a dimer of p11/S100A10 light chains. The light chain, and thus presumably formation of the heterotetramer, was reported to control annexin A2 association to the plasma Membrane and to cortical actin, as well as the distribution of recycling endosomes. However, the specific role of the light chain and the functions of monomeric versus heterotetrameric annexin A2 have remained elusive in the endocytic pathway.

  • The p11/S100A10 light chain of annexin A2 is dispensable for annexin A2 association to endosomes and functions in endosomal transport.
    PLoS ONE, 2007
    Co-Authors: Etienne Morel, Jean Gruenberg
    Abstract:

    Annexin A2 is a Peripheral Membrane Protein that belongs to the annexin family of Ca2+ and phospholipid-binding Proteins. This Protein, which plays a role in Membrane organization and dynamics in particular along the endocytic pathway, exists as a heterotetrameric complex, consisting of two annexin A2 molecules bound via their N-termini to a dimer of p11/S100A10 light chains. The light chain, and thus presumably formation of the heterotetramer, was reported to control annexin A2 association to the plasma Membrane and to cortical actin, as well as the distribution of recycling endosomes. However, the specific role of the light chain and the functions of monomeric versus heterotetrameric annexin A2 have remained elusive in the endocytic pathway.

Gabriele Zanchetti - One of the best experts on this subject based on the ideXlab platform.

  • Sialidase NEU3 is a Peripheral Membrane Protein localized on the cell surface and in endosomal structures.
    Biochemical Journal, 2007
    Co-Authors: Gabriele Zanchetti, Paolo Colombi, Marta Manzoni, Luigi Anastasia, Luigi Caimi, Giuseppe Borsani, Bruno Venerando, Guido Tettamanti, Augusto Preti, Eugenio Monti
    Abstract:

    Sialidase NEU3 is also known as the plasma-Membrane-associated form of mammalian sialidases, exhibiting a high substrate specificity towards gangliosides. In this respect, sialidase NEU3 modulates cell-surface biological events and plays a pivotal role in different cellular processes, including cell adhesion, recognition and differentiation. At the moment, no detailed studies concerning the subcellular localization of NEU3 are available, and the mechanism of its association with cellular Membranes is still unknown. In the present study, we have demonstrated that sialidase NEU3, besides its localization at the plasma Membrane, is present in intracellular structures at least partially represented by a subset of the endosomal compartment. Moreover, we have shown that NEU3 present at the plasma Membrane is internalized and locates then to the recycling endosomal compartment. The enzyme is associated with the outer leaflet of the plasma Membrane, as shown by selective cell-surface Protein biotinylation. This evidence is in agreement with the ability of NEU3 to degrade gangliosides inserted into the plasma Membrane of adjacent cells. Moreover, the mechanism of the Protein association with the lipid bilayer was elucidated by carbonate extraction. Under these experimental conditions, we have succeeded in solubilizing NEU3, thus demonstrating that the enzyme is a Peripheral Membrane Protein. In addition, Triton X-114 phase separation demonstrates further the hydrophilic nature of the Protein. Overall, these results provide important information about the biology of NEU3, the most studied member of the mammalian sialidase family.

  • Sialidase NEU3 is a Peripheral Membrane Protein localized on the cell surface and in endosomal structures
    Biochemical Journal, 2007
    Co-Authors: Gabriele Zanchetti, Paolo Colombi, Marta Manzoni, Luigi Anastasia, Luigi Caimi, Giuseppe Borsani, Bruno Venerando, Guido Tettamanti, Augusto Preti, Eugenio Monti
    Abstract:

    Sialidase NEU3 is also known as the plasma Membrane-associated form of mammalian sialidases, exhibiting a high substrate specificity toward gangliosides. In this respect, sialidase NEU3 modulates cell surface biological events and plays a pivotal role in different cellular processes, including cell adhesion, recognition and differentiation. At the moment, no detailed studies concerning the subcellular localization of NEU3 are available and the mechanism of its association to cellular Membranes is still unknown. Here we demonstrate that sialidase NEU3, besides its localization at the plasma Membrane, is present in intracellular structures at least partially represented by a subset of the endosomal compartment. Moreover, we show that NEU3 present at the plasma Membrane is internalized and locates then to the recycling endosomal compartment. The enzyme is associated to the outer leaflet of the plasma Membrane, as shown by selective cell surface Protein biotinylation. This evidence is in agreement with the ability of NEU3 in degrading gangliosides inserted in the plasma Membrane of adjacent cells. Moreover, the association mechanism of the Protein to the lipid bilayer was elucidated by carbonate extraction. Under these experimental conditions we succeeded in solubilizing NEU3, thus demonstrating that the enzyme is a Peripheral Membrane Protein. In addition, Triton X-114 phase separation further demonstrates the hydrophilic nature of the Protein. Overall, these results provide important information about the biology of NEU3, the most studied member of the mammalian sialidase family.

C. Simone Fishburn - One of the best experts on this subject based on the ideXlab platform.

  • Localization of a Peripheral Membrane Protein: Gβγ targets GαZ
    Proceedings of the National Academy of Sciences of the United States of America, 2000
    Co-Authors: C. Simone Fishburn, Sonia K. Pollitt, Henry R. Bourne
    Abstract:

    To explore the relative roles of Protein-binding partners vs. lipid modifications in controlling Membrane targeting of a typical Peripheral Membrane Protein, Gαz, we directed its binding partner, βγ, to mislocalize on mitochondria. Mislocalized βγ directed wild-type Gαz and a palmitate-lacking Gαz mutant to mitochondria but did not alter localization of a Gαz mutant lacking both myristate and palmitate. Thus, in this paradigm, a Protein–Protein interaction controls targeting of a Peripheral Membrane Protein to the proper compartment, whereas lipid modifications stabilize interactions of Proteins with Membranes and with other Proteins.

  • Localization of a Peripheral Membrane Protein: Gβγ targets GαZ
    Proceedings of the National Academy of Sciences of the United States of America, 2000
    Co-Authors: C. Simone Fishburn, Sonia K. Pollitt, Henry R. Bourne
    Abstract:

    To explore the relative roles of Protein-binding partners vs. lipid modifications in controlling Membrane targeting of a typical Peripheral Membrane Protein, Galpha(z), we directed its binding partner, betagamma, to mislocalize on mitochondria. Mislocalized betagamma directed wild-type Galpha(z) and a palmitate-lacking Galpha(z) mutant to mitochondria but did not alter localization of a Galpha(z) mutant lacking both myristate and palmitate. Thus, in this paradigm, a Protein-Protein interaction controls targeting of a Peripheral Membrane Protein to the proper compartment, whereas lipid modifications stabilize interactions of Proteins with Membranes and with other Proteins.