Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II

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

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

We examined the fine structure of the type I signal-anchor sequence of synaptotagmin II, which has a 60-residue N-terminal domain followed by a hydrophobic region (H-region), focusing on the hinge region between the N-terminal and the H-regions. It was found that the charged or highly polar residues support the translocation of the N-terminal domain through the endoplasmic reticulum membrane at specific positions in the hinge. The residue requirement correlated with the turn propensity scale for transmembranes. It is suggested that a certain conformation, likely helical hairpin, in the hinge is critical for N-terminal domain translocation.

Original languageEnglish
Pages (from-to)341-345
Number of pages5
JournalFEBS Letters
Volume507
Issue number3
DOIs
Publication statusPublished - 2001 Nov 2
Externally publishedYes

Keywords

  • Membrane integration
  • Membrane protein
  • Membrane topology
  • Signal sequence
  • Synaptotagmin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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