Phosphorylation-dependent dimerization and subcellular localization of islet-brain 1/c-Jun N-terminal kinase-interacting protein 1.

Détails

ID Serval
serval:BIB_FE04F42195D0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Phosphorylation-dependent dimerization and subcellular localization of islet-brain 1/c-Jun N-terminal kinase-interacting protein 1.
Périodique
Journal of Neuroscience Research
Auteur(s)
Borsello T., Centeno C., Riederer I.M., Haefliger J.A., Riederer B.M.
ISSN
0360-4012 (Print)
ISSN-L
0360-4012
Statut éditorial
Publié
Date de publication
2007
Peer-reviewed
Oui
Volume
85
Numéro
16
Pages
3632-3641
Langue
anglais
Résumé
Islet-brain 1 [IB1; also termed c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP-1] is involved in the apoptotic signaling cascade of JNK and functions as a scaffold protein. It organizes several MAP kinases and the microtubule-transport motor protein kinesin and relates to other signal-transducing molecules such as the amyloid precursor protein. Here we have identified IB1/JIP-1 using different antibodies that reacted with either a monomeric or a dimeric form of IB1/JIP-1. By immunoelectron microscopy, differences in the subcellular localization were observed. The monomeric form was found in the cytoplasmic compartment and is associated with the cytoskeleton and with membranes, whereas the dimeric form was found in addition in nuclei. After treatment of mouse brain homogenates with alkaline phosphatase, the dimeric form disappeared and the monomeric form decreased its molecular weight, suggesting that an IB1/JIP-1 dimerization is phosphorylation dependent and that IB1 exists in several phospho- forms. N-methyl-D-aspartate receptor activation induced a dephosphorylation of IB1/JIP-1 in primary cultures of cortical neurons and reduced homodimerization. In conclusion, these data suggest that IB1/JIP-1 monomers and dimers may differ in compartmental localization and thus function as a scaffold protein of the JNK signaling cascade in the cytoplasm or as a transcription factor in nuclei.
Mots-clé
Adaptor Proteins, Signal Transducing/metabolism, Animals, Animals, Newborn, Antibody Specificity, Brain/metabolism, Brain/ultrastructure, Cell Compartmentation/physiology, Cell Nucleus/metabolism, Cell Nucleus/ultrastructure, Cytoplasm/metabolism, Cytoplasm/ultrastructure, Cytoskeleton/metabolism, Cytoskeleton/ultrastructure, Dimerization, Immunohistochemistry, Intracellular Membranes/metabolism, Intracellular Membranes/ultrastructure, Mice, Microscopy, Electron, Transmission, Neurons/metabolism, Neurons/ultrastructure, Phosphorylation, Protein Isoforms/metabolism, Rats, Rats, Wistar, Receptors, N-Methyl-D-Aspartate/metabolism, Sus scrofa
Pubmed
Web of science
Création de la notice
24/01/2008 15:34
Dernière modification de la notice
20/08/2019 17:28
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