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

Details

Serval ID
serval:BIB_FE04F42195D0
Type
Article: article from journal or magazin.
Collection
Publications
Title
Phosphorylation-dependent dimerization and subcellular localization of islet-brain 1/c-Jun N-terminal kinase-interacting protein 1.
Journal
Journal of Neuroscience Research
Author(s)
Borsello T., Centeno C., Riederer I.M., Haefliger J.A., Riederer B.M.
ISSN
0360-4012 (Print)
ISSN-L
0360-4012
Publication state
Published
Issued date
2007
Peer-reviewed
Oui
Volume
85
Number
16
Pages
3632-3641
Language
english
Abstract
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.
Keywords
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
Create date
24/01/2008 15:34
Last modification date
20/08/2019 17:28
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