Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 21
pubmed:dateCreated
2001-11-23
pubmed:abstractText
Phosphorylation of neurofascin, a member of the L1 family of cell adhesion molecules (L1 CAMs), at the conserved FIGQY-tyrosine abolishes the ankyrin-neurofascin interaction. This study provides the first evidence, in Drosophila melanogaster and vertebrates, for the physiological occurrence of FIGQY phosphorylation in L1 family members. FIGQY tyrosine phosphorylation is localized at specialized cell junctions, including paranodes of sciatic nerve, neuromuscular junctions of adult rats and Drosophila embryos, epidermal muscle attachment sites of Drosophila, and adherens junctions of developing epithelial cells of rat and Drosophila. In addition, FIGQY-phosphorylated L1 CAMs are abundantly expressed in regions of neuronal migration and axon extension, including the embryonic cortex, the neonatal cerebellum and the rostral migratory stream, a region of continued neurogenesis and migration throughout adulthood in the rat. Based on our results, physiological FIGQY-tyrosine phosphorylation of the L1 family likely regulates adhesion molecule-ankyrin interactions establishing ankyrin-free and ankyrin-containing microdomains and participates in an ankyrin-independent intracellular signaling pathway at specialized sites of intercellular contact in epithelial and nervous tissue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Ankyrins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte L1 Antigen Complex, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Nfasc protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Nrg protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3823-35
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:11719549-Adherens Junctions, pubmed-meshheading:11719549-Amino Acid Sequence, pubmed-meshheading:11719549-Animals, pubmed-meshheading:11719549-Ankyrins, pubmed-meshheading:11719549-Binding Sites, pubmed-meshheading:11719549-Cell Adhesion, pubmed-meshheading:11719549-Cell Adhesion Molecules, pubmed-meshheading:11719549-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:11719549-Cell Movement, pubmed-meshheading:11719549-Central Nervous System, pubmed-meshheading:11719549-Drosophila Proteins, pubmed-meshheading:11719549-Drosophila melanogaster, pubmed-meshheading:11719549-Epithelial Cells, pubmed-meshheading:11719549-Leukocyte L1 Antigen Complex, pubmed-meshheading:11719549-Membrane Glycoproteins, pubmed-meshheading:11719549-Molecular Sequence Data, pubmed-meshheading:11719549-Nerve Growth Factors, pubmed-meshheading:11719549-Neural Cell Adhesion Molecules, pubmed-meshheading:11719549-Neuromuscular Junction, pubmed-meshheading:11719549-Neurons, pubmed-meshheading:11719549-Peptides, pubmed-meshheading:11719549-Phosphorylation, pubmed-meshheading:11719549-Rats, pubmed-meshheading:11719549-Tumor Cells, Cultured, pubmed-meshheading:11719549-Tyrosine
pubmed:year
2001
pubmed:articleTitle
FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons.
pubmed:affiliation
Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA. s.jenkins@cellbio.duke.edu
pubmed:publicationType
Journal Article