Autor: |
Hayato Mizuta, Ayane Takakusaki, Takehiro Suzuki, Keisuke Otake, Naoshi Dohmae, Siro Simizu |
Rok vydání: |
2022 |
Předmět: |
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Zdroj: |
The FEBS journalReferences. 290(1) |
ISSN: |
1742-4658 |
Popis: |
C-mannosylation is a unique type of protein glycosylation via C-C linkage between an α-mannose and a tryptophan residue. This modification has been identified in about 30 proteins and regulates several functions, such as protein secretion and intracellular localization, as well as protein stability. About half of C-mannosylated proteins are categorized as proteins containing thrombospondin type 1 repeat domain or type I cytokine receptors. To evaluate whether C-mannosylation broadly affects protein functions regardless of protein domain or family, we have sought to identify other types of C-mannosylated protein and analyse their functions. In this study, we focused on receptor activity modifying protein 1, which neither contains thrombospondin type 1 repeat domain nor belongs to the type I cytokine receptors. Our mass spectrometry analysis demonstrated that RAMP1 is C-mannosylated at Trp |
Databáze: |
OpenAIRE |
Externí odkaz: |
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