rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5
|
pubmed:dateCreated |
2003-12-9
|
pubmed:abstractText |
The cell adhesion molecule L1 (L1-CAM) plays critical roles in neurite growth. Its cytoplasmic domain (L1CD) binds to ankyrins that associate with the spectrin-actin network. This paper demonstrates that L1-CAM interactions with ankyrinB (but not with ankyrinG) are involved in the initial formation of neurites. In the membranous protrusions surrounding the soma before neuritogenesis, filamentous actin (F-actin) and ankyrinB continuously move toward the soma (retrograde flow). Bead-tracking experiments show that ankyrinB mediates L1-CAM coupling with retrograde F-actin flow in these perisomatic structures. Ligation of the L1-CAM ectodomain by an immobile substrate induces L1CD-ankyrinB binding and the formation of stationary ankyrinB clusters. Neurite initiation preferentially occurs at the site of these clusters. In contrast, ankyrinB is involved neither in L1-CAM coupling with F-actin flow in growth cones nor in L1-based neurite elongation. Our results indicate that ankyrinB promotes neurite initiation by acting as a component of the clutch module that transmits traction force generated by F-actin flow to the extracellular substrate via L1-CAM.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14657231-10462518,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/14657231-9832558
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0021-9525
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
8
|
pubmed:volume |
163
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1077-88
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:14657231-Humans,
pubmed-meshheading:14657231-Animals,
pubmed-meshheading:14657231-Mice,
pubmed-meshheading:14657231-Cerebellum,
pubmed-meshheading:14657231-Neurons,
pubmed-meshheading:14657231-Actins,
pubmed-meshheading:14657231-Ganglia, Spinal,
pubmed-meshheading:14657231-Cell Membrane,
pubmed-meshheading:14657231-Cells, Cultured,
pubmed-meshheading:14657231-Protein Structure, Tertiary,
pubmed-meshheading:14657231-Protein Isoforms
|