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Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum.

Kinectin has been proposed to be a membrane anchor for kinesin on intracellular organelles. A kinectin isoform that lacks a major portion of the kinesin-binding domain does not bind kinesin but interacts with another resident of the endoplasmic reticulum, the translation elongation factor-1 delta (EF-1 delta). This was shown by yeast two-hybrid analysis and a number of in vitro and in vivo assays. EF-1 delta provides the guanine nucleotide exchange activities on EF-1 alpha during elongation step of protein synthesis. The minimal EF-1 delta-binding domain on kinectin resides within a conserved region present in all the kinectin isoforms. Overexpression of the kinectin fragments in vivo disrupted the intracellular localization of EF-1 delta proteins. This report provides evidence of an alternative kinectin function as the membrane anchor for EF-1 delta on the endoplasmic reticulum and provides clues to the EF-1 complex assembly and anchorage on the endoplasmic reticulum.

Pubmed ID: 12773547

Authors

  • Ong LL
  • Er CP
  • Ho A
  • Aung MT
  • Yu H

Journal

The Journal of biological chemistry

Publication Data

August 22, 2003

Associated Grants

None

Mesh Terms

  • Endoplasmic Reticulum
  • Membrane Proteins
  • Peptide Elongation Factor 1
  • Protein Binding
  • Two-Hybrid System Techniques