Expression of NF2-encoded Merlin and Related ERM Family Proteins in the Human Central Nervous System

Stemmer‐Rachamimov, Anat; Gonzalez-Agosti, Charo; Xu, Lin; Burwick, Jennifer A.; Beauchamp, Roberta L.; Pinney, Denise; Louis, David N.; Ramesh, Vijaya

doi:10.1097/00005072-199756060-00011

Cited by 26 publications

(16 citation statements)

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“…Furthermore, the majority of these investigations have been performed with immunofluorescent confocal microscopy, and detailed morphology information on human VS cells can be inferred from these experiments. We found that merlin was expressed in 98% of VS samples, which is in accordance with previous reports that NF2 protein presents in Schwann cells and arachnoidal cells, 14,15,22,23 whereas others reported different results showing total merlin absence. 24,25 In our study, trypsin was used to digest the tissue slices to improve the binding of primary antibody to the proteins.…”

Section: Discussionsupporting

confidence: 92%

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Compensative Shuttling of Merlin to Phosphorylation on Serine 518 in Vestibular Schwannoma

Zou

et al. 2008

The Laryngoscope

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Section: Discussionsupporting

confidence: 92%

“…Endogenous merlin was expressed in schwannoma cells of 98% of patients, which is in line with earlier reports. 14,15 However, some cells demonstrated strong nuclear staining and others weak perinuclear staining (Fig. 1G).…”

Section: Confirmation Of Merlin Expression In Vs Samples and Normal Vmentioning

confidence: 97%

Compensative Shuttling of Merlin to Phosphorylation on Serine 518 in Vestibular Schwannoma

Zou

et al. 2008

The Laryngoscope

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“…Interestingly, CD44 also binds ERMs and its association with either ERMs or schwannomin seems to correspond to different stages of Schwann cells proliferation (Morrison et al 2001). Schwannomin is also widely expressed in neurons (Claudio et al 1995;Stemmer-Rachamimov et al 1997;den Bakker et al 1999; our own observations), but its neuronal partners are so far unknown. Thus, paranodin is the first neuronal transmembrane protein reported to be associated with schwannomin.…”

Section: (A) (B)mentioning

confidence: 60%

Association of Caspr/paranodin with tumour suppressor schwannomin/merlin and β1 integrin in the central nervous system

Denisenko-Nehrbass

Goutebroze

Galvez

et al. 2003

Journal of Neurochemistry

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Caspr/paranodin is an essential neuronal component of paranodal axoglial junctions, associated with contactin/F3. Its short intracellular domain contains a conserved motif (GNP motif) capable of binding protein 4.1 domains [FERM domains (four point one, ezrin, radixin, moesin)]. Schwannomin/merlin is a tumour suppressor expressed in many cell types, including in neurons, the function and partners of which are still poorly characterized. We show that the FERM domain of schwannomin binds to the paranodin GNP motif in glutathione S-transferase (GST)-pull down assays and in transfected COS-7 cells. The two proteins co-immunoprecipitated in brain extracts. In addition, paranodin and schwannomin were associated with integrin b 1 in transfected cells and in brain homogenates. The presence of paranodin increased the association between integrin b 1 and schwannomin or its N-terminal domain, suggesting that the interactions between these proteins are interdependent. In jimpy mutant mice, which display a severe dysmyelination with deficient paranodal junctions, the interactions between paranodin, schwannomin and integrin b 1 were profoundly altered. Our results show that schwannomin and integrin b 1 can be associated with paranodin in the central nervous system. Since integrin b 1 and schwannomin do not appear to be enriched in paranodes they may be quantitatively minor partners of paranodin in these regions and/or be associated with paranodin at other locations.

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“…Although expression of ezrin was first characterized in epithelial tissues (Bretscher, 1983), several studies have since indicated the expression of ezrin and related molecules in the nervous system of mammals and birds (Goslin et al, 1989;Everett & Nichol, 1990;Birgbauer et al, 1991;Böhling et al, 1996;Gonzalez-Agosti & Solomon, 1996;Stemmer-Rachamimov et al, 1997). However, some of the antibodies used in these studies were not specific for ezrin, and immunohistochemical analyses in neural tissues have not been performed sufficiently.…”

Section: Distribution Of Ezrin In Other Neural Tissuesmentioning

confidence: 99%

Specific expression of ezrin, a cytoskeletal‐membrane linker protein, in a subset of chick retinotectal and sensory projections

Takahashi

Yamagata

Noda

1999

Eur J of Neuroscience

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Lamina-specific neuronal connections are a fundamental feature in many parts of the vertebrate central nervous system. In the chick, the optic tectum is the primary visual centre, and it has a multilaminated structure consisting of 15 laminae, of which only three or four receive retinal projections. Each of the retinorecipient laminae establishes synaptic connections selectively from one of a few subsets of retinal ganglion cells (RGCs). We have generated a series of monoclonal antibodies that appear to stain only one of the retinorecipient laminae. One of these, TB4, stained lamina F which receives inputs from a subpopulation of approximately 10-20% of RGCs which express the presynaptic acetylcholine receptor beta2-subunit. TB4 recognized a single 79-kDa protein on immunoblotting. cDNA cloning and immunochemical analysis revealed that the TB4 antigen molecule was ezrin, a cytoskeletal-membrane linker molecule belonging to the ezrin-radixin-moesin family. Unilateral enucleation of the eye, both prior to and after the establishment of retinotectal projections, attenuated the lamina-selective staining with TB4 in the contralateral tectum, suggesting that ezrin is anterogradely transported from RGCs to lamina F. Ezrin was thus expressed in a subset of RGCs that project to lamina F. Similar subset-selective expression and resultant lamina-selective distribution of ezrin were also observed in the lamina-specific central projections from the dorsal root ganglia. The staining pattern with TB4 in the dorsal root ganglia and spinal cord indicated that high expression of ezrin was restricted in cutaneous sensory neurons, but not in muscle sensory neurons. Since ezrin modulates cell morphology and cell adhesion profiles by linking membrane proteins with the cytoskeleton, it was suggested that ezrin is involved in the formation and/or maintenance of lamina-specific connections for neuronal subpopulations in the visual and somatosensory systems.

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Expression of NF2-encoded Merlin and Related ERM Family Proteins in the Human Central Nervous System

Cited by 26 publications

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Compensative Shuttling of Merlin to Phosphorylation on Serine 518 in Vestibular Schwannoma

Compensative Shuttling of Merlin to Phosphorylation on Serine 518 in Vestibular Schwannoma

Association of Caspr/paranodin with tumour suppressor schwannomin/merlin and β1 integrin in the central nervous system

Specific expression of ezrin, a cytoskeletal‐membrane linker protein, in a subset of chick retinotectal and sensory projections

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