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Data on the effect of knockout of neruregulin-1 type III on Remak bundle structure.

ABSTRACT: Schwann cells in the peripheral nervous system wrap around large diameter axons to form the myelin sheath, that contains one axon. Schwann cells also wrap around small diameter axons to form the Remak bundle, that contains many axons. Neuregulin-1 (NRG1) type III binds Schwann cell plasma membrane ErbB2/3 receptor to regulate morphological changes of Schwann cells. Herein we provide the data on the effect of NRG1 type III knockout (Miyamoto et al., 2017) [1] on the Remak bundle structure. Since complete knockout mice of NRG1type III are embryonically lethal, we have usedNRG1type III (+/-) mice's sciatic nerves in these experiments.

SUBMITTER: Miyamoto Y

PROVIDER: S-EPMC5996742 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Data on the effect of knockout of neruregulin-1 type III on Remak bundle structure.

Miyamoto Yuki Y Torii Tomohiro T Inoue Masashi M Morimoto Takako T Yamamoto Masahiro M Yamauchi Junji J

Data in brief 20180327

Schwann cells in the peripheral nervous system wrap around large diameter axons to form the myelin sheath, that contains one axon. Schwann cells also wrap around small diameter axons to form the Remak bundle, that contains many axons. Neuregulin-1 (NRG1) type III binds Schwann cell plasma membrane ErbB2/3 receptor to regulate morphological changes of Schwann cells. Herein we provide the data on the effect of NRG1 type III knockout (Miyamoto et al., 2017) [1] on the Remak bundle structure. Since ...[more]

PMID: 29900241

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Project description:Type III adenylyl cyclase (AC3, ADCY3) is predominantly enriched in neuronal primary cilia throughout the central nervous system (CNS). Genome-wide association studies in humans have associated ADCY3 with major depressive disorder and autistic spectrum disorder, both of which exhibit sexual dimorphism. To date, it is unclear how AC3 affects protein phosphorylation and signal networks in central neurons, and what causes the sexual dimorphism of autism. We employed a mass spectrometry (MS)-based phosphoproteomic approach to quantitatively profile differences in phosphorylation between inducible AC3 knockout (KO) and wild type (WT), male and female mice. In total, we identified 4,655 phosphopeptides from 1,756 proteins, among which 565 phosphopeptides from 322 proteins were repetitively detected in all samples. Over 46% phosphopeptides were identified in at least three out of eight biological replicas. Comparison of AC3 KO and WT datasets revealed that phosphopeptides with motifs matching proline-directed kinases' recognition sites had a lower abundance in the KO dataset than in WTs. We detected 14 phosphopeptides restricted to WT dataset (i.e., Rabl6, Spast and Ppp1r14a) and 35 exclusively in KOs (i.e., Sptan1, Arhgap20, Arhgap44, and Pde1b). Moreover, 95 phosphopeptides (out of 90 proteins) were identified only in female dataset and 26 only in males. Label-free MS spectrum quantification using Skyline further identified phosphopeptides that had higher abundance in each sample group. In total, 204 proteins had sex-biased phosphorylation and 167 of them had increased expression in females relative to males. Interestingly, among the 204 gender-biased phosphoproteins, 31% were found to be associated with autism, including Dlg1, Dlgap2, Syn1, Syngap1, Ctnna1, Ctnnd1, Ctnnd2, Pkp4, and Arvcf. Therefore, this study also provides the first phosphoproteomics evidence suggesting that gender-biased post-translational phosphorylation may be implicated in the sexual dimorphism of autism.

Dataset Information

Data on the effect of knockout of neruregulin-1 type III on Remak bundle structure.

Publications

Data on the effect of knockout of neruregulin-1 type III on Remak bundle structure.

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