Journal
GENE EXPRESSION PATTERNS
Volume 4, Issue 1, Pages 77-84Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S1567-133X(03)00146-7
Keywords
synapse; neuromuscular junction; acetylcholine receptors; muscle-specific receptor tyrosine kinase; ubiquitination; E3 ubiquitin ligase; ariadne; yeast-two-hybrid
Categories
Ask authors/readers for more resources
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. (C) 2003 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available