| RRC ID |
73126
|
| Author |
Mizuta H, Takakusaki A, Suzuki T, Otake K, Dohmae N, Simizu S.
|
| Title |
C-mannosylation regulates stabilization of RAMP1 protein and RAMP1-mediated cell migration.
|
| Journal |
FEBS J
|
| Abstract |
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.
|
| Published |
2022-8-9
|
| DOI |
10.1111/febs.16592
|
| PMID |
35942636
|
| IF |
4.392
|
| Resource |
| DNA material |
CSII-CMV-MCS-IRES2-Bsd (RDB04385)
Genome Network Project Human cDNA Clone IRAL005C15 (HGY082063) |
