Phorboxazole analogues induce association of cdk4 with extranuclear cytokeratin intermediate filaments
Craig J Forsyth1, Lu Ying, Jiehao Chen
1Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, USA. forsyth@chem.umn.edu
Abstract:
The cellular localization profile and molecular association of the phorboxazoles were examined with a streamlined target elucidation system using synthetic fluorescent probes. Cellular image analyses identified the binding of phorboxazole analogues to cytosolic components. Proteomic analysis directed at fluorescently labeled cytosolic fractions indicated that the primary targets observed microscopically were cytokeratins, as verified by determination of low nanomolar binding to cloned and expressed proteins. Phorboxazole probes localized the essential cell cycle promoter cdk4 upon cytokeratin networks.
More Related Videos
13:15Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
Published on: February 25, 2016
06:00Through the Looking Glass: Time-lapse Microscopy and Longitudinal Tracking of Single Cells to Study Anti-cancer Therapeutics
Published on: May 14, 2016
Related Concept Videos
Positive Regulator Molecules
Positive Regulator Molecules
Inhibition of Cdk Activity
M-Cdk Drives Transition Into Mitosis
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
Inhibition of CDK Activity
M-Cdk Drives Transition Into Mitosis
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
