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Updated: Jul 17, 2026

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
Published on: December 10, 2016
Identification of ER membrane targeting signal of kinectin
Erika Abe1, Satoshi Okawa, Masashiro Sugawara
1Department of Neurology, Akita University School of Medicine, 1-1-1 Hondo, Akita 010-8543, Japan. erikaa@doc.med.akita-u.ac.jp
Abstract:
Kinectin has been identified as a kinesin receptor on endoplasmic reticulum (ER). The ER membrane binding domain of kinectin is still obscure and is thought to require a half of the molecule. To determine the ER insertion site, we produced several constructs around N-terminus of kinectin connected with green fluorescent protein (GFP) and visualized the distribution in Cos-7 cells. The fragment of residues 7-29 appeared in the reticular pattern exactly colocalized with the ER marker but did not remain for a long time. On the other hand, residues 1-106 maintained a reticular pattern for more than seven days. These results indicate that residues 7-29 of kinectin are sufficient for targeting to the ER membrane but insufficient for remaining on the ER.
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