Periaxin, a novel protein of myelinating schwann cells with a possible role in axonal ensheathment

Gillespie, C S; Sherman, Diane L.; Blair, G. Eric; Brophy, Peter

doi:10.1016/0896-6273(94)90208-9

Cited by 160 publications

(143 citation statements)

References 55 publications

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“…This suggests that PRX alters the role in the stage of myelination and plays significant roles in the formation and maintenance of myelin and in the signal transduction from the extracellular matrix to the cytoskeleton of myelinating Schwann cells. L-periaxin has four characteristic domains: PDZ, NLS, repeat and acidic domains (Gillespie et al 1994;Sherman and Brophy 2000;Sherman et al 2001). To date, nine pedigrees, carrying ten nonsense or frameshift mutations of PRX, have been reported (Boerkoel et al 2001;Guilbot et al 2001;Takashima et al 2002;Kijima et al 2004).…”

Section: Discussionmentioning

confidence: 99%

Periaxin mutation in Japanese patients with Charcot-Marie-Tooth disease

et al. 2006

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Periaxin (PRX) plays an important role in the myelination of the peripheral nerve and consequently in the pathogenesis of Charcot-Marie-Tooth disease (CMT). To date, nine nonsense or frameshift PRX mutations have been reported in eight families with CMT. The patients with PRX mutations appeared to show characteristic clinical features with early onset but slow or no progression, a common result of mutations that lead to missing a C-terminal acidic domain. Here, we report a Japanese CMT patient with these characteristic clinical features, who was a compound heterozygote for PRX R1070X and L132FsX153 mutations. We previously reported that three Japanese isolated families also had the homozygous R1070X mutation. To examine the potential founder effect of the R1070X mutation in the Japanese population, we performed haplotype analysis and found that each R1070X allele lay on a different haplotype background in these four families. Therefore, the high frequency of the R1070X mutation among the Japanese population is not likely the consequence of a founder effect, but probably a result of a mutation hot spot.

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Section: Discussionmentioning

confidence: 99%

Periaxin mutation in Japanese patients with Charcot-Marie-Tooth disease

et al. 2006

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“…As a preliminary analysis of these sites, ChIP assays were performed to test binding of Egr2 to two of the novel candidate sites in both the S16 Schwann cell line (Hai et al, 2002), and in freshly dissected sciatic nerves of rat pups (postnatal day 15). The site in the periaxin gene (located within the first intron, ~4.5 kb downstream of the transcription start site) was chosen because its expression depends on Egr2 (Parkinson et al, 2003) and is developmentally regulated in a manner similar to the Mpz gene (Gillespie et al, 1994). In addition, the Mag upstream site was chosen because our previous work has detected binding of Egr2 to the intronassociated site at +1552 LeBlanc et al, 2007).…”

Section: Identification Of Evolutionarily Conserved Sox/egr2 Binding mentioning

confidence: 99%

Interactions of Sox10 and Egr2 in myelin gene regulation

et al. 2007

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Myelination in the PNS is accompanied by a large induction of the Myelin Protein Zero (Mpz) gene to produce the most abundant component in peripheral myelin. Analyses of knockout mice have shown that the EGR2/Krox20 and SOX10 transcription factors are required for Mpz expression. Our recent work has shown that the dominant EGR2 mutations associated with human peripheral neuropathies cause disruption of EGR2/SOX10 synergy at specific sites, including a conserved enhancer element in the first intron of the Mpz gene. Further investigation of Egr2/Sox10 interactions reveals that activation of the Mpz intron element by Egr2 requires both Sox10-binding sites. In addition, both Egr1 and Egr3 cooperate with Sox10 to activate this element, which indicates that this capacity is conserved among Egr family members. Finally, a conserved composite structure of Egr2/ Sox10-binding sites in the genes encoding Mpz, Myelin-associated glycoprotein (Mag), and Myelin Basic Protein (Mbp) genes was used to screen for similar modules in other myelin genes, revealing a potential regulatory element in the periaxin gene. Overall, these results elucidate a working model for developmental regulation of Mpz expression, several facets of which extend to regulation of other peripheral myelin genes.

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“…tein kinase A (Weinman et al, 1995), and single copies in rhophilin (Watanabe et al, 1996), periaxin (Gillespie et al, 1994), PICK1 (Staudinger et al, 1995), enigma (Wu & Gill, 1994), human APXlike protein (Schiaffino et al, 1995), CLP36 , and Ritl8 . A human gene product (KIAA0147) contains leucine-rich repeats and 4 PDZs (Nagase et al, 1995).…”

Section: Novel Eukaryotic Pdz Domainsmentioning

confidence: 99%

Evidence for PDZ domains in bacteria, yeast, and plants

1997

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Several dozen signaling proteins are now known to contain 80-100 residue repeats, called PDZ (or DHR or GLGF) domains, several of which interact with the C-terminal tetrapeptide motifs X-Ser/Thr-X-Val-COO-of ion channels and/or receptors. PDZ domains have previously been noted only in mammals, flies, and worms, suggesting that the primordial PDZ domain arose relatively late in eukaryotic evolution. Here, techniques of sequence analysis-including local alignment, profile, and motif database searches-indicate that PDZ domain homologues are present in yeast, plants, and bacteria. It is suggested that two PDZ domains occur in bacterial high-temperature requirement A (htrA) and one in tail-specific protease (tsp) homologues, and that a yeast htrA homologue contains four PDZ domains. Sequence comparisons suggest that the spread of PDZ domains in these diverse organisms may have occurred via horizontal gene transfer. The known affinity of Escherichia coli tsp for C-terminal polypeptides is proposed to be mediated by its PDZ-like domain, in a similar manner to the binding of C-terminal polypeptides by animal PDZ domains.

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Periaxin, a novel protein of myelinating schwann cells with a possible role in axonal ensheathment

Cited by 160 publications

References 55 publications

Periaxin mutation in Japanese patients with Charcot-Marie-Tooth disease

Periaxin mutation in Japanese patients with Charcot-Marie-Tooth disease

Interactions of Sox10 and Egr2 in myelin gene regulation

Evidence for PDZ domains in bacteria, yeast, and plants

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