Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/14929
Title: Characterization the role of kinectin in assembly of translation elongation complex to endoplasmic reticulum and its involvement in organelle motility
Authors: ONG LEE LEE
Keywords: Kinectin, translation elongation factors, endoplasmic reticulum, kinesin, protein synthesis, alternate splicing
Issue Date: 17-Nov-2005
Source: ONG LEE LEE (2005-11-17). Characterization the role of kinectin in assembly of translation elongation complex to endoplasmic reticulum and its involvement in organelle motility. ScholarBank@NUS Repository.
Abstract: Kinectin has been initially proposed to be a membrane anchor for kinesin. We found evidences to kinectina??s alternative function as the membrane anchor for EF-1I' on the endoplasmic reticulum. Over-expression of the kinectin fragments in vivo disrupted the intracellular localization of EF-1I' proteins. Since EF-1 exists as a quaternary complex, we next characterized the assembly of the whole complex to ER via kinectin. Our results suggest the anchorage of EF-1I?I?I' complex to ER is via kinectin instead of EF-1I?I? interacts with other regions of the ER membrane in kinectin- and EF-1I'- independent manners. We have observed that kinectin down-regulate and upregulate membraneous and cytosolic protein synthesis respectively. We have also demonstrated by RNA interference assay that kinectin is involved in the intracellular dynamics of ER and mitochondria. Together with well-documented role of kinectin-kinesin interaction in intracellular transport of ER and lysosomes, we confirm the role of kinectin in organelle motility.
URI: http://scholarbank.nus.edu.sg/handle/10635/14929
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