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.
Ong
Lee-Lee
LL
National University Medical Institutes and Department of Physiology, Faculty of Medicine, National University of Singapore, Singapore 117597.
Er
Connie P N
CP
Ho
Andrea
A
Aung
May T
MT
Yu
Hanry
H
D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D020648:Peptide Elongation Factor 1 / Q000378:metabolism*; D011485:Protein Binding; D020798:Two-Hybrid System Techniques
C088547:KTN1 protein, human; D008565:Membrane Proteins; D020648:Peptide Elongation Factor 1