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Updated: Sep 8, 2025

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
GAS2L1 facilitates Golgi-derived microtubule growth and Golgi organization
Bill K T Hau1, Khoi T D Le1, Franco K C Au1
1Division of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Abstract:
The Golgi complex serves as a major noncentrosomal microtubule-organizing center in animal cells, with Golgi-derived microtubules playing a crucial role in Golgi assembly, structural organization, cell migration, and various Golgi-related cellular functions. In this study, we identify GAS2L1 as a key regulator of Golgi-based microtubule growth and Golgi reassembly. Loss of GAS2L1 leads to significant defects in Golgi morphology and impairs nocodazole washout-induced Golgi reassembly. Notably, microtubule regrowth from the Golgi after nocodazole treatment is markedly inhibited in GAS2L1-knockout cells. Furthermore, we demonstrate that GAS2L1 interacts with CLASP1/2, known regulators of Golgi-derived microtubules, suggesting that GAS2L1 functions in concert with CLASP1/2 to regulate Golgi-associated microtubule dynamics. These findings provide new insights into the molecular mechanisms governing Golgi-derived microtubules, expanding our understanding beyond the established roles of CLASP1/2.
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