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dc.contributor.authorMakarov, Dmytro -
dc.date.accessioned2023-11-21T03:09:04Z-
dc.date.available2023-11-21T03:09:04Z-
dc.date.issued2023-
dc.identifier.otherOER000002663vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/23527-
dc.description.abstractTubulin detyrosination-tyrosination cycle regulates the stability of microtubules. Thus far described on α-tubulins, the tyrosination level is maintained by a single tubulin-tyrosine ligase (TTL). However, the precise dynamics and tubulin isoforms which undergo (de)tyrosination in neurons are unknown. Here, we exploit the substrate promiscuity of the TTL to introduce an O-propargyl-L-tyrosine in neuroblastoma cells and neurons. Mass spectrometry-based chemical proteomics in neuroblastoma cells using the O-propargyl-L-tyrosine probe revealed previously discussed tyrosination of TUBA4A, MAPRE1, and other non-tubulin proteins. This finding was further corroborated in differentiating neurons. Together we present the method for tubulin tyrosination profiling in living cells. Our results show that detyrosination-tyrosination is not restricted to α-tubulins with coded C-terminal tyrosine and is thus involved in fine-tuning of the tubulin and non-tubulin proteins during neuronal differentiation.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2022.07.02.498566v1.full.pdf+htmlvi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherbioRxivvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectProteomicsvi
dc.subjecthóa họcvi
dc.subjecttyros hóavi
dc.subjectproteinvi
dc.subjectAlpha-Tubulinvi
dc.subjecttế bào ngườivi
dc.subject.lccTP248.3vi
dc.titleChemical Proteomics Reveals Protein Tyrosination Extends Beyond the Alpha-Tubulins in Human Cellsvi
dc.typeJournal articlevi
dc.description.noteCC BY-NC-ND 4.0vi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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