A functional FERM domain binding motif in neurofascin

Gunn-Moore, Frank J.; Hill, Maria; Davey, Fleur; Herron, Lissa R.; Tait, Steven; Sherman, Diane L.; Brophy, Peter

doi:10.1016/j.mcn.2006.09.003

Cited by 19 publications

(15 citation statements)

References 35 publications

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“…To establish where Willin is located within the sciatic nerve, we compared the mRNA expression pattern of Willin with the Schwann cell expressing isoform of the transmembrane receptor neurofascin [33] by in situ hybridization. The Willin transcript appeared to be predominately located at the perineurium (the periphery) of the sciatic nerve (Figure 1A), but also within discrete cells within the endoneurium.…”

Section: Resultsmentioning

confidence: 99%

Willin, an Upstream Component of the Hippo Signaling Pathway, Orchestrates Mammalian Peripheral Nerve Fibroblasts

et al. 2013

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Willin/FRMD6 was first identified in the rat sciatic nerve, which is composed of neurons, Schwann cells, and fibroblasts. Willin is an upstream component of the Hippo signaling pathway, which results in the inactivation of the transcriptional co-activator YAP through Ser127 phosphorylation. This in turn suppresses the expression of genes involved in cell growth, proliferation and cancer development ensuring the control of organ size, cell contact inhibition and apoptosis. Here we show that in the mammalian sciatic nerve, Willin is predominantly expressed in fibroblasts and that Willin expression activates the Hippo signaling cascade and induces YAP translocation from the nucleus to the cytoplasm. In addition within these cells, although it inhibits cellular proliferation, Willin expression induces a quicker directional migration towards scratch closure and an increased expression of factors linked to nerve regeneration. These results show that Willin modulates sciatic nerve fibroblast activity indicating that Willin may have a potential role in the regeneration of the peripheral nervous system.

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Section: Resultsmentioning

confidence: 99%

Willin, an Upstream Component of the Hippo Signaling Pathway, Orchestrates Mammalian Peripheral Nerve Fibroblasts

et al. 2013

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“…The ability of NF155 to direct the formation of the paranode and stabilize the complex formation suggests that it may interact with cytoskeletal proteins. Although no protein-binding partners have been identified, it has been shown that the intracellular domain of NF155 contains a FERM domain-binding motif (Gunn-Moore et al 2006). Given that FERM domain-containing proteins are cytoskeletal linkers, NF155 may coordinate signals originating from the axon that direct changes in the glial cytoskeleton prior to and during myelination; whereby, axonal domains are partitioned.…”

Section: Axonal Domains Of Myelinated Axonsmentioning

confidence: 99%

Myelination and Regional Domain Differentiation of the Axon

Thaxton

Bhat

2009

Results and Problems in Cell Differentiation

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During evolution, as organisms increased in complexity and function, the need for the ensheathment and insulation of axons by glia became vital for faster conductance of action potentials in nerves. Myelination, as the process is termed, facilitates the formation of discrete domains within the axolemma that are enriched in ion channels, and macromolecular complexes consisting of cell adhesion molecules and cytoskeletal regulators. While it is known that glia play a substantial role in the coordination and organization of these domains, the mechanisms involved and signals transduced between the axon and glia, as well as the proteins regulating axo-glial junction formation remain elusive. Emerging evidence has shed light on the processes regulating myelination and domain differentiation, and key molecules have been identified that are required for their assembly and maintenance. This review highlights these recent findings, and relates their significance to domain disorganization as seen in several demyelinating disorders and other neuropathies.

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“…Thus the SAX-7 FB domain may provide an additional or alternative means to link SAX-7 to the actin cytoskeleton and signaling pathways. L1 and neurofascin have been shown to bind ezrin (Dickson et al 2002;Gunn-Moore et al 2006). Among the multiple FERM proteins present in C. elegans is a single ezrin homolog that is encoded by the erm-1 gene (Göbel et al 2004;Van Fürden et al 2004).…”

Section: Unc-44 and Sax-7 Are Not Interdependent For Protein Localizamentioning

confidence: 99%

“…The L1CAM cytoplasmic tail contains several highly conserved motifs that include a protein 4.1, ezrin, radixin, moesin (FERM)-binding domain, an ankyrin-binding domain, and a PSD 95, disc-large, ZO1 (PDZ)-binding motif (Davis and Bennett 1994;Koroll et al 2001;Dickson et al 2002;Gunn-Moore et al 2006). Of these domains, the ankyrin-binding domain is well characterized and has been shown to directly bind ankyrin, an adaptor protein that links diverse membrane proteins to the spectrin-actin cytoskeleton (Davis and Bennett 1994).…”

mentioning

confidence: 99%

unc-44 Ankyrin and stn-2 γ-Syntrophin Regulate sax-7 L1CAM Function in Maintaining Neuronal Positioning in Caenorhabditis elegans

Zhou¹,

Opperman²,

Wang

et al. 2008

Genetics

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The L1 family of single-pass transmembrane cell adhesion molecules (L1CAMs) is conserved from Caenorhabditis elegans and Drosophila to vertebrates and is required for axon guidance, neurite outgrowth, and maintenance of neuronal positions. The extracellular region of L1CAMs mediates cell adhesion via interactions with diverse cell-surface and extracellular matrix proteins. In contrast, less is known regarding the function of the intracellular domains in the L1CAM cytoplasmic tail. Previously, we identified a role of the C. elegans L1CAM homolog, SAX-7, in maintaining neuronal and axonal positioning. Here, we demonstrate that this function is dependent on three conserved motifs that reside in the SAX-7 cytoplasmic tail: (1) the FERM-binding motif, (2) the ankyrin-binding domain, and (3) the PDZ-binding motif. Furthermore, we provide molecular and genetic evidence that UNC-44 ankyrin and STN-2 g-syntrophin bind SAX-7 via the respective ankyrin-binding and PDZ-binding motifs to regulate SAX-7 function in maintaining neuronal positioning.

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A functional FERM domain binding motif in neurofascin

Cited by 19 publications

References 35 publications

Willin, an Upstream Component of the Hippo Signaling Pathway, Orchestrates Mammalian Peripheral Nerve Fibroblasts

Willin, an Upstream Component of the Hippo Signaling Pathway, Orchestrates Mammalian Peripheral Nerve Fibroblasts

Myelination and Regional Domain Differentiation of the Axon

unc-44 Ankyrin and stn-2 γ-Syntrophin Regulate sax-7 L1CAM Function in Maintaining Neuronal Positioning in Caenorhabditis elegans

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