DOI: 10.1083/jcb.142.6.1571. Restriction of 480/270-kD Ankyrin G to Axon Proximal Segments Requires Multiple Ankyrin G-specific Domains

Restriction of 480/270-kD Ankyrin G to Axon Proximal Segments Requires Multiple Ankyrin G-specific Domains

10.1083/jcb.142.6.1571

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

AnkyrinG (−/−) neurons fail to concentrate voltage-sensitive sodium channels and neurofascin at their axon proximal segments, suggesting that ankyrinG is a key component of a structural pathway involved in assembly of specialized membrane domains at axon proximal segments and possibly nodes of Ranvier (Zhou, D., S. Lambert, D.L. Malen, S. Carpenter, L. Boland, and V. Bennett, manuscript submitted for publication). This paper addresses the mechanism for restriction of 270-kD ankyrinG to axon proximal segments by evaluation of localization of GFP-tagged ankyrinG constructs transfected into cultured dorsal root ganglion neurons, as well as measurements of fluorescence recovery after photobleaching of neurofascin– GFP-tagged ankyrinG complexes in nonneuronal cells. A conclusion is that multiple ankyrinG-specific domains, in addition to the conserved membrane-binding domain, contribute to restriction of ankyrinG to the axonal plasma membrane in dorsal root ganglion neurons. The ankyrinG-specific spectrin-binding and tail domains are capable of binding directly to sites on the plasma membrane of neuronal cell bodies and axon proximal segments, and presumably have yet to be identified docking sites. The serine-rich domain, which is present only in 480- and 270-kD ankyrinG polypeptides, contributes to restriction of ankyrinG to axon proximal segments as well as limiting lateral diffusion of ankyrinG–neurofascin complexes. The membrane-binding, spectrin-binding, and tail domains of ankyrinG also contribute to limiting the lateral mobility of ankyrinG–neurofascin complexes. AnkyrinG thus functions as an integrated mechanism involving cooperation among multiple domains heretofore regarded as modular units. This complex behavior explains ability of ankyrinB and ankyrinG to sort to distinct sites in neurons and the fact that these ankyrins do not compensate for each other in ankyrin gene knockouts in mice.

Bibliography

Zhang, X., & Bennett, V. (1998). Restriction of 480/270-kD AnkyrinâG to Axon Proximal Segments Requires Multiple AnkyrinâG-specific Domains. The Journal of Cell Biology, 142(6), 1571â1581.

Authors 2

Xu Zhang (first)
Vann Bennett (additional)

References 41 Referenced 114

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{'key': '2023072207581976500_B5', 'first-page': '107', 'article-title': 'Molecular architecture of the specialized axonal membrane at the node of Ranvier', 'volume': '52', 'author': 'Bennett', 'year': '1997', 'journal-title': 'Soc Gen Physiol Ser'} / Soc Gen Physiol Ser / Molecular architecture of the specialized axonal membrane at the node of Ranvier by Bennett (1997)
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{'key': '2023072207581976500_B40'}
{'key': '2023072207581976500_B41'}

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 22, 2023, 3:59 a.m.)
Indexed	1 month, 4 weeks ago (July 7, 2025, 2:02 a.m.)
Issued	26 years, 11 months ago (Sept. 21, 1998)
Published	26 years, 11 months ago (Sept. 21, 1998)
Published Online	26 years, 11 months ago (Sept. 21, 1998)
Published Print	26 years, 11 months ago (Sept. 21, 1998)

Funders 0

None

BibTeX

@article{Zhang_1998, title={Restriction of 480/270-kD Ankyrin G to Axon Proximal Segments Requires Multiple Ankyrin G-specific Domains}, volume={142}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.142.6.1571}, DOI={10.1083/jcb.142.6.1571}, number={6}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Zhang, Xu and Bennett, Vann}, year={1998}, month=sep, pages={1571–1581} }

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