C. Vanoni
University of Milan
6 Papers
83 Citations
C. Vanoni is an academic researcher from University of Milan. The author has contributed to research in topics: PDZ domain & Membrane protein. The author has an hindex of 6, co-authored 6 publications.
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Papers
Increased internalisation and degradation of GLT-1 glial glutamate transporter in a cell model for familial amyotrophic lateral sclerosis (ALS)
C. Vanoni,Silvia Massari,Marco Losa,Paolo Carrega,Carla Perego,Laura Conforti,Grazia Pietrini +6 more
TL;DR: The data indicate that the continuous expression of mutant SOD1 causes the downregulation of GLT-1 by increasing the internalisation and degradation of the surface transporter, and suggest that the cytosolic tail of GLt-1 is required to target the transporter to degradation.
Protein Kinase C-mediated Phosphorylation of the BGT1 Epithelial γ-Aminobutyric Acid Transporter Regulates Its Association with LIN7 PDZ Proteins A POST-TRANSLATIONAL MECHANISM REGULATING TRANSPORTER SURFACE DENSITY
TL;DR: In this article, a protein kinase C (PKC)-mediated mechanism regulating the association between BGT1 and LIN7 was described, where reduced transport activity paralleled by the intracellular relocalization of the transporter was observed in response to the PKC activation induced by 12-Otetradecanoylphorbol-13-acetate (TPA) treatment.
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Mammalian LIN‐7 PDZ proteins associate with β‐catenin at the cell–cell junctions of epithelia and neurons
TL;DR: It is reported here that mammalian LIN‐7 PDZ proteins form a complex with cadherin and β‐catenin in epithelia and neurons and suggests the mechanism by which β‐ catenin mediates the organization of the junctional domain.
The GLT-1 and GLAST glutamate transporters are expressed on morphologically distinct astrocytes and regulated by neuronal activity in primary hippocampal cocultures.
TL;DR: The data indicate that soluble factors dependent on neuronal activity play a major regulating role in hippocampal cocultures and soluble factors in neuronal‐conditioned media prevented the down‐regulation of the GLT‐1 and GLAST proteins.
PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells.
Carla Perego,C. Vanoni,Antonello Villa,Renato Longhi,Susan M. Kaech,Erika Fröhli,Alex Hajnal,Stuart K. Kim,Grazia Pietrini +8 more
TL;DR: Interactions with PDZ proteins determine the polarized surface localization of target proteins by means of retention and not targeting mechanisms, and may act as a sort of membrane protein sorting machinery which, by recognizing retention signals (the PDZ target sequences), prevents protein internalization.