Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum

Yuichiro Kida, Masao Sakaguchi, Mitsunori Fukuda, Katsuhiko Mikoshiba, Katsuyoshi Mihara

研究成果: Article査読

45 被引用数 (Scopus)

抄録

Synaptotagmin II is a type I signal-anchor protein, in which the NH2-terminal domain of 60 residues (N-domain) is located within the lumenal space of the membrane and the following hydrophobic region (H-region) shows transmembrane topology. We explored the early steps of cotranslational integration of this molecule on the endoplasmic reticulum membrane and demonstrated the following: (a) The translocation of the N-domain occurs immediately after the H-region and the successive positively charged residues emerge from the ribosome. (b) Positively charged residues that follow the H-region are essential for maintaining the correct topology. (c) It is possible to dissect the lengths of the nascent polypeptide chains which are required for ER targeting of the ribosome and for translocation of the N-domain, thereby demonstrating that different nascent polypeptide chain lengths are required for membrane targeting and N-domain translocation. (d) The H-region is sufficiently long for membrane integration. (e) Proline residues preceding H-region are critical for N-domain translocation, but not for ER targeting. The proline can be replaced with amino acid with low helical propensity.

本文言語English
ページ(範囲)719-729
ページ数11
ジャーナルJournal of Cell Biology
150
4
DOI
出版ステータスPublished - 2000 8月 21
外部発表はい

ASJC Scopus subject areas

  • 細胞生物学

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