A putative ariadne-like E3 ubiquitin ligase (PAUL) that interacts with the muscle-specific kinase (MuSK)

Formation of the postsynaptic membrane at the skeletal neuromuscular junction (NMJ) requires activation of the muscle-specific receptor tyrosine kinase (MuSK). Few intracellular mediators or modulators of MuSK actions are known. E3 ubiquitin ligases may serve this role, because activities of several...

Full description

Saved in:
Bibliographic Details
Published in:Gene Expression Patterns 2004, Vol.4 (1), p.77-84
Main Authors: Bromann, Paul A., Weiner, Joshua A., Apel, Elizabeth D., Lewis, Renate M., Sanes, Joshua R.
Format: Article
Language:English
Subjects:
Acetylcholine receptors
Amino Acid Sequence
Animals
Ariadne
Blotting, Northern
Brain - embryology
Brain - metabolism
Cell Line
E3 ubiquitin ligase
Gene Expression Profiling
Gene Expression Regulation, Developmental
Gene Expression Regulation, Enzymologic
Humans
In Situ Hybridization
Kidney - embryology
Kidney - metabolism
Liver - embryology
Liver - metabolism
Lung - cytology
Lung - embryology
Lung - metabolism
Mice
Molecular Sequence Data
Muscle, Skeletal - cytology
Muscle, Skeletal - embryology
Muscle, Skeletal - metabolism
Muscle-specific receptor tyrosine kinase
MuSK protein
Myocardium - cytology
Myocardium - metabolism
Neuromuscular junction
PAUL protein
Phylogeny
Precipitin Tests
Protein Binding
Receptor Protein-Tyrosine Kinases - genetics
Receptor Protein-Tyrosine Kinases - metabolism
Receptors, Cholinergic - genetics
Receptors, Cholinergic - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Synapse
Two-Hybrid System Techniques
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Yeast-two-hybrid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Formation of the postsynaptic membrane at the skeletal neuromuscular junction (NMJ) requires activation of the muscle-specific receptor tyrosine kinase (MuSK). Few intracellular mediators or modulators of MuSK actions are known. E3 ubiquitin ligases may serve this role, because activities of several receptor tyrosine kinases, G-protein-coupled receptors and channels are modulated by ubiquitination. Here, we report identification of a putative Ariadne-like ubiquitin ligase (PAUL) that binds to the cytoplasmic domain of MuSK. PAUL is expressed in numerous tissues of developing and adult mice, and is present at NMJs in muscle fibers but is not confined to them.
ISSN:1567-133X
1872-7298
DOI:10.1016/S1567-133X(03)00146-7