Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape

Intrinsically disordered myelin basic protein (MBP) is one of the key autoantigens in autoimmune neurodegeneration and multiple sclerosis particularly. MBP is highly positively charged and lacks distinct structure in solution and therefore its intracellular partners are still mostly enigmatic. Here...

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Autores principales:	Evgeniya V. Smirnova, Tatiana V. Rakitina, Rustam H. Ziganshin, Georgij P. Arapidi, George A. Saratov, Anna A. Kudriaeva, Alexey A. Belogurov
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	myelin basic protein MBP interactome formaldehyde cross-linking MS-based proteomic analysis Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/f67732b8105d4ffe9e1f67bb806b847b
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id	oai:doaj.org-article:f67732b8105d4ffe9e1f67bb806b847b
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spelling	oai:doaj.org-article:f67732b8105d4ffe9e1f67bb806b847b2021-11-25T16:53:00ZComprehensive Atlas of the Myelin Basic Protein Interaction Landscape10.3390/biom111116282218-273Xhttps://doaj.org/article/f67732b8105d4ffe9e1f67bb806b847b2021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1628https://doaj.org/toc/2218-273XIntrinsically disordered myelin basic protein (MBP) is one of the key autoantigens in autoimmune neurodegeneration and multiple sclerosis particularly. MBP is highly positively charged and lacks distinct structure in solution and therefore its intracellular partners are still mostly enigmatic. Here we used combination of formaldehyde-induced cross-linking followed by immunoprecipitation and liquid chromatography-tandem mass spectrometry (LC-MS/MS) to elucidate the interaction network of MBP in mammalian cells and provide the list of potential MBP interacting proteins. Our data suggest that the largest group of MBP-interacting proteins belongs to cellular proteins involved in the protein translation machinery, as well as in the spatial and temporal regulation of translation. MBP interacts with core ribosomal proteins, RNA helicase Ddx28 and RNA-binding proteins STAU1, TDP-43, ADAR-1 and hnRNP A0, which are involved in various stages of RNA biogenesis and processing, including specific maintaining MBP-coding mRNA. Among MBP partners we identified CTNND1, which has previously been shown to be necessary for myelinating Schwann cells for cell-cell interactions and the formation of a normal myelin sheath. MBP binds proteins MAGEB2/D2 associated with neurotrophin receptor p75NTR, involved in pathways that promote neuronal survival and neuronal death. Finally, we observed that MBP interacts with RNF40–a component of heterotetrameric Rnf40/Rnf20 E3 ligase complex, recruited by Egr2, which is the central transcriptional regulator of peripheral myelination. Concluding, our data suggest that MBP may be more actively involved in myelination not only as a main building block but also as a self-regulating element.Evgeniya V. SmirnovaTatiana V. RakitinaRustam H. ZiganshinGeorgij P. ArapidiGeorge A. SaratovAnna A. KudriaevaAlexey A. BelogurovMDPI AGarticlemyelin basic proteinMBPinteractomeformaldehyde cross-linkingMS-based proteomic analysisMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1628, p 1628 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	myelin basic protein MBP interactome formaldehyde cross-linking MS-based proteomic analysis Microbiology QR1-502
spellingShingle	myelin basic protein MBP interactome formaldehyde cross-linking MS-based proteomic analysis Microbiology QR1-502 Evgeniya V. Smirnova Tatiana V. Rakitina Rustam H. Ziganshin Georgij P. Arapidi George A. Saratov Anna A. Kudriaeva Alexey A. Belogurov Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
description	Intrinsically disordered myelin basic protein (MBP) is one of the key autoantigens in autoimmune neurodegeneration and multiple sclerosis particularly. MBP is highly positively charged and lacks distinct structure in solution and therefore its intracellular partners are still mostly enigmatic. Here we used combination of formaldehyde-induced cross-linking followed by immunoprecipitation and liquid chromatography-tandem mass spectrometry (LC-MS/MS) to elucidate the interaction network of MBP in mammalian cells and provide the list of potential MBP interacting proteins. Our data suggest that the largest group of MBP-interacting proteins belongs to cellular proteins involved in the protein translation machinery, as well as in the spatial and temporal regulation of translation. MBP interacts with core ribosomal proteins, RNA helicase Ddx28 and RNA-binding proteins STAU1, TDP-43, ADAR-1 and hnRNP A0, which are involved in various stages of RNA biogenesis and processing, including specific maintaining MBP-coding mRNA. Among MBP partners we identified CTNND1, which has previously been shown to be necessary for myelinating Schwann cells for cell-cell interactions and the formation of a normal myelin sheath. MBP binds proteins MAGEB2/D2 associated with neurotrophin receptor p75NTR, involved in pathways that promote neuronal survival and neuronal death. Finally, we observed that MBP interacts with RNF40–a component of heterotetrameric Rnf40/Rnf20 E3 ligase complex, recruited by Egr2, which is the central transcriptional regulator of peripheral myelination. Concluding, our data suggest that MBP may be more actively involved in myelination not only as a main building block but also as a self-regulating element.
format	article
author	Evgeniya V. Smirnova Tatiana V. Rakitina Rustam H. Ziganshin Georgij P. Arapidi George A. Saratov Anna A. Kudriaeva Alexey A. Belogurov
author_facet	Evgeniya V. Smirnova Tatiana V. Rakitina Rustam H. Ziganshin Georgij P. Arapidi George A. Saratov Anna A. Kudriaeva Alexey A. Belogurov
author_sort	Evgeniya V. Smirnova
title	Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
title_short	Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
title_full	Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
title_fullStr	Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
title_full_unstemmed	Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape
title_sort	comprehensive atlas of the myelin basic protein interaction landscape
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f67732b8105d4ffe9e1f67bb806b847b
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Comprehensive Atlas of the Myelin Basic Protein Interaction Landscape

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