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Title:The Effect of Lanthionine Ketimine on CRMP1’s Ability to Control Actin Assembly
Author(s):Yang, Ran
Contributor(s):Brieher, William M.
Subject(s):Cell and Developmental Biology
Actin cytoskeleton
Collapsin Response Mediator Protein 1
Lanthionine Ketimine
Abstract:The actin cytoskeleton is an essential component for cell shape and function. Yet our understanding of how cells control actin assembly is still limited. Studies have found that a family of proteins, known as Collapsin Response Mediator Proteins (CRMPs), control the actin cytoskeleton network in various cell processes. A member of this family, CRMP1, has been found to play a role in axonogenesis, cancer cell metastasis suppression, and the regulation of cell migration and cell-cell adhesion in kidney epithelial cells. In addition, a small molecule naturally abundant in the human brain, lanthionine ketimine (LK), has been found to directly bind to CRMP2, but this binding interaction has not been quantified and its physiological significance is not yet known. Based on ~75% shared sequence identity of CRMP1 and CRMP2, LK likely interacts with CRMP1 and influences the ability of CRMP1 to regulate actin assembly. Now, the binding interaction between CRMP1 and LK is discovered and quantified, and a maximal binding of LK is found to increase the interaction between CRMP1 and filamentous actin (F-actin).
Issue Date:2018
Type:Image
URI:http://hdl.handle.net/2142/101856
Rights Information:Copyright 2018 Ran Yang
Date Available in IDEALS:2018-10-15


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