Related Experiment Video
Updated: Aug 9, 2026

Super-Resolution Live Cell Imaging of Subcellular Structures
Published on: January 13, 2021
Analysis of structure and microtubule assembly activity of the Drosophila 205K MAP
I Irminger-Finger1, R Ortega Perez
1Division of Oncology, University of Geneva Medical Center, Switzerland.
Abstract:
Phosphorylation, dimerization and binding to calmodulin have been reported to influence the microtubule assembly capacities of MAPs (microtubule-associated proteins). Here we report that the Drosophila 205K MAP is a phosphoprotein in vivo and can be phosphorylated by cdc2/p34 in vitro. Bacterially produced 205K MAP is competent of microtubule assembly and microtubule bundling and binds to immobilized calmodulin in a Ca2+-dependent way. EM rotary shadowing analyses suggest that 205K MAP consists of an amino-terminal flexible extended region and a carboxy-terminal globular domain. This carboxy-terminal region harbors the microtubule binding site and sequences required for dimerization, as confirmed by in vitro crosslinking experiments of truncated proteins.
Related Concept Videos
Microtubule Formation
Microtubule Associated Proteins (MAPs)
Assembly of Complex Microtubule Structures
Microtubules in Cell Motility
Microtubule Instability
Spindle Assembly
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a microtubule array...

