A Conserved Role for L1 as a Transmembrane Link Between Neuronal Adhesion and Membrane Cytoskeleton Assembly

Hortsch, Michael; O’Shea, K. Sue; Zhao, Guangyan; Kim, F.; Vallejo, Yolanda; Dubreuil, Ronald R.

doi:10.3109/15419069809005599

Cited by 50 publications

(52 citation statements)

References 31 publications

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“…Interaxonal fasciculation in the peduncle probably involves binding to and stabilization by the actin cytoskeleton network via the ankyrin-binding domain shared by the two NRG isoforms. This conclusion is supported by previous aggregation experiments in Drosophila S2 cells in which it was shown that homophilic binding of NRG leads to recruitment of ankyrin to the contact sites (Dubreuil et al, 1996;Hortsch et al, 1998b) and by the observation that RNAi-mediated knockdown of neuron-specific ank2-RNA results in MB phenotypes similar to those seen in Nrg mutants (T.G. and P.C., unpublished).…”

Section: Discussionsupporting

confidence: 68%

The Drosophila L1CAM homolog Neuroglian signals through distinct pathways to control different aspects of mushroom body axon development

et al. 2011

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SUMMARYThe spatiotemporal integration of adhesion and signaling during neuritogenesis is an important prerequisite for the establishment of neuronal networks in the developing brain. In this study, we describe the role of the L1-type CAM Neuroglian protein (NRG) in different steps of Drosophila mushroom body (MB) neuron axonogenesis. Selective axon bundling in the peduncle requires both the extracellular and the intracellular domain of NRG. We uncover a novel role for the ZO-1 homolog Polychaetoid (PYD) in axon branching and in sister branch outgrowth and guidance downstream of the neuron-specific isoform NRG-180. Furthermore, genetic analyses show that the role of NRG in different aspects of MB axonal development not only involves PYD, but also TRIO, SEMA-1A and RAC1.

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Section: Discussionsupporting

confidence: 68%

The Drosophila L1CAM homolog Neuroglian signals through distinct pathways to control different aspects of mushroom body axon development

et al. 2011

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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 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).…”

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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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“…L ICAM-mediated cell adhesion is stabilized through the interaction with ankyrin, which links LlCAMs to the spectrin-actin cytoskeleton. LI and neuroglian can interact with cytoskeletal ankyrin and recruit ankyrin to the cell-cell contact sites by LI-mediated cell adhesion (Dubreuil et al, 1996;Hortsch et al, 1998b). This interaction is important for the closed monomer opened monomer blocked monomer Fig.…”

Section: The LI Subfamily Of Camsmentioning

confidence: 99%

Posttranslational processing and functional analysis of Tractin, an L1 family member in leech

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A Conserved Role for L1 as a Transmembrane Link Between Neuronal Adhesion and Membrane Cytoskeleton Assembly

Cited by 50 publications

References 31 publications

The Drosophila L1CAM homolog Neuroglian signals through distinct pathways to control different aspects of mushroom body axon development

The Drosophila L1CAM homolog Neuroglian signals through distinct pathways to control different aspects of mushroom body axon development

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

Posttranslational processing and functional analysis of Tractin, an L1 family member in leech

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