DNA Sequence, genomic organization, and chromosomal localization of the mouse peripheral myelin protein zero gene: Identification of polymorphic alleles

You, Kwang Ho; Hsieh, Chih Lin; Hayes, Carol; Stahl, Norbert; Francke, Uta; Popko, Brian

doi:10.1016/0888-7543(91)90370-t

Cited by 34 publications

(15 citation statements)

References 19 publications

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“…A member of the immunoglobulin-like superfamily, P0 (28–30 KDa) is codified as a type I transmembrane protein from the MPZ gene (D'Urso et al, 1990; You et al, 1991; Hayasaka et al, 1993). Abundantly and specifically expressed by myelinating Schwann cells, P0 protein alone represents 20–50% of all PNS myelin proteins (Everly et al, 1973; Greenfield et al, 1973; Patzig et al, 2011).…”

Section: Erqc and Charcot-marie-tooth (Cmt) Neuropathiesmentioning

confidence: 99%

Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders

Volpi¹,

Touvier²,

D’Antonio³

2017

Front. Mol. Neurosci.

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Reaching the correct three-dimensional structure is crucial for the proper function of a protein. The endoplasmic reticulum (ER) is the organelle where secreted and transmembrane proteins are synthesized and folded. To guarantee high fidelity of protein synthesis and maturation in the ER, cells have evolved ER-protein quality control (ERQC) systems, which assist protein folding and promptly degrade aberrant gene products. Only correctly folded proteins that pass ERQC checkpoints are allowed to exit the ER and reach their final destination. Misfolded glycoproteins are detected and targeted for degradation by the proteasome in a process known as endoplasmic reticulum-associated degradation (ERAD). The excess of unstructured proteins in the ER triggers an adaptive signal transduction pathway, called unfolded protein response (UPR), which in turn potentiates ERQC activities in order to reduce the levels of aberrant molecules. When the situation cannot be restored, the UPR drives cells to apoptosis. Myelin-forming cells of the central and peripheral nervous system (oligodendrocytes and Schwann cells) synthesize a large amount of myelin proteins and lipids and therefore are particularly susceptible to ERQC failure. Indeed, deficits in ERQC and activation of ER stress/UPR have been implicated in several myelin disorders, such as Pelizaeus-Merzbacher and Krabbe leucodystrophies, vanishing white matter disease and Charcot-Marie-Tooth neuropathies. Here we discuss recent evidence underlying the importance of proper ERQC functions in genetic disorders of myelinating glia.

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Section: Erqc and Charcot-marie-tooth (Cmt) Neuropathiesmentioning

confidence: 99%

Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders

Volpi¹,

Touvier²,

D’Antonio³

2017

Front. Mol. Neurosci.

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“…In the last two decades, sequences of P0 from different species have been reported, including Rattus norvegicu: rat (Lemke and Axel, 1985), Bos taurus: bovine (Sakamoto et al, 1987), Heterodontus francisci: Horn shark (Saavedra et al, 1989), Gallus gallus: chicken (Barbu, 1990), Homo sapiens: human (Hayasaka et al, 1991), Mus musculus: mouse (You et al, 1991), Salmo sp. : trout (Stratmann and Jeserich, 1995), and Danio rerio: zebrafish (Schweitzer et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Peripheral myelin of Xenopus laevis: Role of electrostatic and hydrophobic interactions in membrane compaction

Luo

Cerullo

Dawli

et al. 2008

Journal of Structural Biology

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P0 glycoprotein is the major structural protein of peripheral nerve myelin where it is thought to modulate inter-membrane adhesion at both the extracellular apposition, which is labile upon changes in pH and ionic strength, and the cytoplasmic apposition, which is resistant to such changes. Most studies on P0 have focused on structure-function correlates in higher vertebrates. Here, we focused on its role in the structure and interactions of frog (Xenopus laevis) myelin, where it exists primarily in a dimeric form. As part of our study, we deduced the full sequence of Xenopus laevis P0 (xP0) from its cDNA. The xP0 sequence was found to be similar to P0 sequences of higher vertebrates, suggesting that a common mechanism of PNS myelin compaction via P0 interaction might have emerged through evolution. As previously reported for mouse PNS myelin, a similar change of extracellular apposition in frog PNS myelin as a function of pH and ionic strength was observed, which can be explained by a conformational change of P0 due to protonation-deprotonation of His52 at P0's putative adhesive interface. On the other hand, the cytoplasmic apposition in frog PNS myelin, like that in the mouse, remained unchanged at different pH and ionic strength. The contribution of hydrophobic interactions to stabilizing the cytoplasmic apposition was tested by incubating sciatic nerves with detergents. Dramatic expansion at the cytoplasmic apposition was observed for both frog and mouse, indicating a common hydrophobic nature at this apposition. Urea also expanded the cytoplasmic apposition of frog myelin likely owing to denaturation of P0. Removal of the fatty acids that attached to the single Cys residue in the cytoplasmic domain of P0 did not change PNS myelin structure of either frog or mouse, suggesting that the P0-attached fatty acyl chain does not play a significant role in PNS myelin compaction and stability. These results help clarify the present understanding of P0's adhesion role and the role of its acylation in compact PNS myelin.

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“…Therefore, we reasoned that a comparison of the mammalian MBP (Takahashi et al, 1985;Popko et al, 1988;Miura et al, 1989;Boylan et al, 1990) and Po (Lemke et al? 1988;You et a]., 1991) promoters to their corresponding counterparts in shark could help to identify DNA sequences essential for the regulated expression of these genes. We have reported previously the cloning and sequence of the shark Po promoter (Fors et al, 1990).…”

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confidence: 99%

Sequence Similarities of Myelin Basic Protein Promoters from Mouse and Shark: Implications for the Control of Gene Expression in Myelinating Cells

Fors

Hood

Saavedra

1993

Journal of Neurochemistry

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Abstract:To better understand the cell type-specific and coordinated regulation of the myelin protein genes, we cloned and sequenced the shark myelin basic protein (MBP) promoter. An alignment of the shark sequence with the corresponding mouse sequence showed striking similarities. These similarities, together with the results from expression experiments, define two major regions (A and B) within the MBP promoter. Region A is located immediately 5' to the transcription initiation sites and includes five sequences thought to be cis-acting domains. These domains include two boxes of 13 and 12 nucleotides, respectively, separated from each other by 10 nucleotides, an MBP enhancer, and GC, CCAAT, and TATA boxes. Region A also contains a putative exon that codes for 35 amino acids of an unidentified polypeptide. Region B, which is located adjacent to the 5' end of region A, contains two boxes that are 10 and 1 I nucleotides long, respectively, and are identical in mouse and shark. We have previously cloned and sequenced the shark glycoprotein zero (Po) promoter. A comparison between the sequences of the rat and shark Po promoters shows three conserved regions in addition to CCAAT and TATA boxes. The shark Po promoter is active in the CNS and PNS, and contains a sequence of 13 nucleotides that is located at -159 from the initiation of transcription and is similar to that of the MBP enhancer. The mammalian Po promoter is active exclusively in the adult PNS and contains a sequence similar to that of the MBP enhancer located adjacent to the 3' side of the transcription initiation site. Sequence similarities and differences between the promoters of the mammalian and shark myelin protein genes will help to identify the basis for the cell type-specific and coordinated expression of these genes. Key Words: Myelin protein genes-Myelin basic protein promoter-Po promoter. Fors L. et al. Sequence similarities of myelin basic protein promoters from mouse and shark: Implications for the control ofgene expression in myelinating cells. J. Neurochern. 60, 513-521 (1993).

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DNA Sequence, genomic organization, and chromosomal localization of the mouse peripheral myelin protein zero gene: Identification of polymorphic alleles

Cited by 34 publications

References 19 publications

Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders

Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders

Peripheral myelin of Xenopus laevis: Role of electrostatic and hydrophobic interactions in membrane compaction

Sequence Similarities of Myelin Basic Protein Promoters from Mouse and Shark: Implications for the Control of Gene Expression in Myelinating Cells

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