Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2067971 | Cell Biology International | 2006 | 10 Pages |
Abstract
Kinectin (KNT) is a candidate membrane receptor for kinesin in the movement of intracellular organelles along microtubules. Isoforms of KNT exist containing different combinations of six small (residues 23-33) variable domains (vd) vd1-6 within the C-terminus. Here we investigate a role for KNT and its isoform KNTvd4â in the transport of amylin and insulin-containing secretory vesicles in the pancreatic islet β-cell line RINm5F. KNTvd4â lacks vd4 that forms the kinesin-binding domain, and hence its role in the cell is an enigma. We report that amylin-containing vesicles also contained insulin, and exhibited microtubule, and small G-protein-dependent secretion. Knockdown of KNT by small interference RNA (siRNA) inhibited amylin expression and secretion. In contrast, recombinant KNTvd4â overexpressed in RINm5F cells associated with amylin-containing vesicles and inhibited amylin secretion, but had no discernible affect on amylin expression. The data suggests that both KNT and KNTvd4â participate in microtubule-dependent secretion of amylin in islet β-cells.
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Authors
Ji-Zhong Bai, Yu Mon, Geoffrey W. Krissansen,