Cis-activation of L1-mediated Ankyrin Recruitment by TAG-1 Homophilic Cell Adhesion

Malhotra, Jyoti; Tsiotra, Panayoula C.; Καραγωγεωσ, Δομνα; Hortsch, Michael

doi:10.1074/jbc.273.50.33354

Cited by 78 publications

(61 citation statements)

References 35 publications

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“…Following homophilic binding, CAMs of the L1 family transduce signals resulting in the recruitment of ankyrin and spectrin to points of cell-cell contact (13)(14)(15)(16)(17). Drosophila S2 cells are a classic model system in which potential CAMs have been tested for these properties (14,27).…”

Section: Resultsmentioning

confidence: 99%

“…These antibodies were described in a previous publication (11). Mouse anti-Drosophila ankyrin antibodies were generated as described previously (17). ␣-Amanitin was obtained from Sigma.…”

Section: Methodsmentioning

confidence: 99%

“…These results suggested that sodium channel ␤ subunits function as CAMs. CAMs of the L1 family also bind directly to cytoskeletal elements such as ankyrin (12,13,(15)(16)(17). Sodium channels have been shown to colocalize with ankyrin G and spectrin at axon initial segments and nodes of Ranvier, and there is some evidence to show that sodium channels bind ankyrin directly in vitro (18 -22).…”

mentioning

confidence: 99%

“…Ankyrins associate via their membrane binding domains with several ion channels and cell adhesion molecules of the L1 family (12)(13)(14)(15)(16)(17). The membrane binding domain of ankyrin contains four subdomains that are each composed of six ankyrin repeats (24).…”

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confidence: 99%

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Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact

Malhotra¹,

Kazen-Gillespie²,

Hortsch³

et al. 2000

Journal of Biological Chemistry

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Sodium channels isolated from mammalian brain are composed of ␣, ␤1, and ␤2 subunits. The auxiliary ␤ subunits do not form the ion conducting pore, yet play important roles in channel modulation and plasma membrane expression. ␤1 and ␤2 are transmembrane proteins with one extracellular V-set immunoglobulin (Ig) protein domain. It has been shown recently that ␤1 and ␤2 interact with the extracellular matrix proteins tenascin-C and tenascin-R. In the present study we show that rat brain ␤1 and ␤2, but not ␣IIA, subunits interact in a trans-homophilic fashion, resulting in recruitment of the cytoskeletal protein ankyrin to sites of cell-cell contact in transfected Drosophila S2 cells. Whereas ␣IIA subunits expressed alone do not cause cellular aggregation, ␤ subunits co-expressed with ␣IIA retain the ability to adhere and recruit ankyrin. Truncated ␤ subunits lacking cytoplasmic domains interact homophilically to produce cell aggregation but do not recruit ankyrin. Thus, the cytoplasmic domains of ␤1 and ␤2 are required for cytoskeletal interactions. It is hypothesized that sodium channel ␤ subunits serve as a critical communication link between the extracellular and intracellular environments of the neuron and may play a role in sodium channel placement at nodes of Ranvier.Control of the cell surface density and localization of voltagegated sodium channels are critical aspects of neuronal function. This is especially important at nodes of Ranvier of myelinated axons where high densities of sodium channels are needed for rapid and reliable saltatory conduction (1, 2). Sodium channels from mammalian brain are heterotrimeric structures composed of a central pore forming ␣ subunit and two auxiliary subunits, ␤1 and ␤2 (3, 4). Though the ␤ subunits do not form the ion conducting pore, they play critical roles in channel gating, voltage dependence of activation and inactivation, and channel plasma membrane expression levels (5-8). ␤1 and ␤2 contain Ig-like extracellular domains and are members of the V-set of the Ig superfamily, which includes many cell adhesion molecules (CAMs) 1 (9). ␤1 and ␤2 have recently been shown to interact with the extracellular matrix proteins tenascin-C and tenascin-R (10, 11). Transfected cells expressing ␤1 or ␤2 subunits initially bind to and then are repelled from a tenascin-R substrate (11). Purified sodium channels or the bacterially expressed ␤2 subunit extracellular domain bind tenascin-C and tenascin-R in an enzyme-linked immunosorbent type biochemical assay (10). These results suggested that sodium channel ␤ subunits function as CAMs. CAMs of the L1 family also bind directly to cytoskeletal elements such as ankyrin (12,13,(15)(16)(17). Sodium channels have been shown to colocalize with ankyrin G and spectrin at axon initial segments and nodes of Ranvier, and there is some evidence to show that sodium channels bind ankyrin directly in vitro (18 -22). However, it is not known to which sodium channel subunit ankyrin binds. Because ␤1 and ␤2 are structurally and functionally homologous ...

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Section: Resultsmentioning

confidence: 99%

“…These antibodies were described in a previous publication (11). Mouse anti-Drosophila ankyrin antibodies were generated as described previously (17). ␣-Amanitin was obtained from Sigma.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact

Malhotra¹,

Kazen-Gillespie²,

Hortsch³

et al. 2000

Journal of Biological Chemistry

Self Cite

260

281

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show abstract

“…In general, it has been shown that ankyrinB binding promotes neuritogenesis by coupling L1CAM to the actin cytoskeleton (Nishimura et al, 2003). Binding L1CAM to ankyrinG, conversely, is thought to recruit L1CAM to the AIS, a highly specialized compartment in the proximal axon where APs are generated (Malhotra et al, 1998;Yoshimura and Rasband, 2014). Both ankyrins are thought to recruit and compartmentalize L1CAM and other L1CAM family members, such as neurofascin Boiko et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Conditional deletion of L1CAM in human neurons impairs both axonal and dendritic arborization and action potential generation

Patzke¹,

Acuña²,

Giam³

et al. 2016

J Cell Biol

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Cellular signaling by neural cell adhesion molecules of the immunoglobulin superfamily

2000

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Cis-activation of L1-mediated Ankyrin Recruitment by TAG-1 Homophilic Cell Adhesion

Abstract: Neural cell adhesion molecules (CAMs) of the immunoglobulin (Ig) superfamily mediate not only cell aggregation but also growth cone guidance and neurite outgrowth. In this study we demonstrate that two neural CAMs, L1-CAM and TAG-1, induce the homophilic aggregation of Drosophila

Cited by 78 publications

References 35 publications

Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact

Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact

Conditional deletion of L1CAM in human neurons impairs both axonal and dendritic arborization and action potential generation

Cellular signaling by neural cell adhesion molecules of the immunoglobulin superfamily

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