Linked Life Data

16122940

Source:http://linkedlifedata.com/resource/pubmed/id/16122940

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-9-19
pubmed:abstractText
Non-myelinating perisynaptic Schwann cells wrap motor axon terminals and are required for both functional and structural integrity of the neuromuscular junction. Several lines of evidence indicate that fine-tuning of neuregulin-1/ErbB signaling is critical for maintaining perisynaptic Schwann cells at synapses and that this control may be achieved by the developmental downregulation of the ErbB2 receptor. Here, we identify a direct interaction between ErbB2 and LNX1, an E3 ubiquitin ligase that can target interacting proteins for degradation through ubiquitination. Immunostaining shows that LNX1 is specifically localized in perisynaptic Schwann cells but not in Schwann cells along the motor axon. Developmentally, levels of LNX1 protein are inversely correlated with the responsiveness of perisynaptic Schwann cells to neuregulin-1. Furthermore, the LNX1 staining disappears upon denervation, whereas ErbB2 reappears in Schwann cells after denervation. Taken together, these data suggest that LNX1 may play a role in regulating neuregulin-1/ErbB signaling in perisynaptic Schwann cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1044-7431
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
238-48
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
LNX1 is a perisynaptic Schwann cell specific E3 ubiquitin ligase that interacts with ErbB2.
pubmed:affiliation
Department of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't