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We observed new mechanisms of microtubule nucleation regulation.
Microtubules act as railways inside the cell, guiding molecular motors that transport cargo along them. Microtubules originate from centrosomes, which control when and how each microtubule grows. This nucleation requires small protein complexes containing g-tubulin (g-TuRCs). This project explored newly identified g-tubulin-binding proteins, previously known for their ability to form tri-complexes, playing a role in cell cortex regulation. Identifying the specific roles of each protein within this tri-complex and how they individually interact with gamma-tubulin, this work deepened our understanding of how spatially separated reactions are functionally interconnected and regulate microtubule nucleation.
Distribution of microtubules across cytoplasm of human cell
Distribution of microtubules across cytoplasm of human cell
Microtubules are nucleated from centrosome
Microtubules are nucleated from centrosome
Centrosome matrix binds
microtubule nucleation rings
(g-TuRCs)
Credit: Schnackenberg et al., 1998
How is microtubule nucleation from the centrosome regulated? What are the main interacting partners of gTuRCs, microtubule nucleation complexes at the centrosome?
Microtubule nucleation complex (gTuRCs) within centrosome
Blue = g-tubulin, grey = tubulin dimers of microtubule
Credit: the Lüders lab
See more in Cernohorska et al., 2016, Sulimenko et al., 2015, and the following papers
While PIX and GIT keep g-tubulin in closed conformation, unable for phosphorylation, PAK kinase activates it and removes PIX from GIT, increasing microtubule nucleation from the centrosome.
While PIX and GIT keep g-tubulin in closed conformation, unable for phosphorylation, PAK kinase activates it and removes PIX from GIT, increasing microtubule nucleation from the centrosome.
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