期刊
JOURNAL OF CELL BIOLOGY
卷 162, 期 6, 页码 1161-1172出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200305078
关键词
TAG-1/axonin-1/contactin-2; paranodin/Caspr/NCP-1; potassium channels; protein 4.1B; nodes of Ranvier
类别
资金
- NINDS NIH HHS [R01 NS39346-01, R01 NS039346] Funding Source: Medline
Myelination results in a highly segregated distribution of axonal membrane proteins at nodes of Ranvier. Here, we show the role in this process of TAG-1, a glycosyl-phosphatidyl-inositol-anchored cell adhesion molecule. In the absence of TAG-1, axonal Caspr2 did not accumulate at juxtaparanodes, and the normal enrichment of shaker-type K+ channels in these regions was severely disrupted, in the central and peripheral nervous systems. in contrast, the localization of protein 4.1 B, an axoplasmic partner of Caspr2, was only moderately altered. TAG-1, which is expressed in both neurons and glia, was able to associate in cis with Caspr2 and in trans with itself. Thus, a tripartite intercellular protein complex, comprised of these two proteins, appears critical for axo-glial contacts at juxtaparanodes. This complex is analogous to that described previously at paranodes, suggesting that similar molecules are crucial for different types of axo-glial interactions.
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