C-mannosylation regulates stabilization of RAMP1 protein and RMAP1-mediated cell migration

Hayato Mizuta, Ayane Takakusaki, Takehiro Suzuki, Keisuke Otake, Naoshi Dohmae, Siro Simizu

研究成果: Article査読

抄録

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 Trp56. It has been shown that RAMP1 transports to the plasma membrane after dimerization with calcitonin receptor-like receptor and is important for ligand-dependent downstream signalling activation. Our results showed that C-mannosylation has no effect on this transport activity. On the other hand, C-mannosylation did enhance protein stability and cell migration activity. Our data may provide new insight into both C-mannosylation research and novel RAMP1 analysis.

本文言語English
ジャーナルFEBS Journal
DOI
出版ステータスAccepted/In press - 2022

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

フィンガープリント

「C-mannosylation regulates stabilization of RAMP1 protein and RMAP1-mediated cell migration」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル