Multimeric conformation of type III intermediate filaments but not the filamentous conformation exhibits high affinity to lipid bilayers

Beomju Hwang, Hirohiko Ise

研究成果: ジャーナルへの寄稿学術誌査読

10 被引用数 (Scopus)

抄録

Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin, classified as the type III intermediate filament family, maintain the integrity and architecture of various cell types. Recently, we reported their cell surface expression and binding to multivalent N-acetylglucosamine-conjugated polymers. Furthermore, the presence of vimentin on the surface of various cell types including malignant tumor cells and fibroblasts has been demonstrated. Type III intermediate filament proteins are traditionally considered intracellular proteins and do not possess signal peptides for cell membrane recruitment. Therefore, the mechanism of their transport to the cell surface is unclear. In the current study, we aimed to elucidate this mechanism by focusing on the relationship between their multimeric structure and lipid bilayer affinity. Blue native polyacrylamide gel electrophoresis demonstrated that cell surface-expressed type III intermediate filament proteins formed a multimeric mostly including 4–12-mers but not filamentous structure. Moreover, surface plasmon resonance analysis revealed that the multimeric structure of these recombinant proteins had high affinity to lipid bilayers, whereas their filament-like large multimeric structure did not. Our results suggest that type III intermediate filaments are incorporated into the cell membrane through alteration from a filamentous to a multimeric structure.

本文言語英語
ページ(範囲)413-426
ページ数14
ジャーナルGenes to Cells
25
6
DOI
出版ステータス出版済み - 6月 1 2020

!!!All Science Journal Classification (ASJC) codes

  • 遺伝学
  • 細胞生物学

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