Abstract:
:Tau is a neuronal microtubule-associated protein found predominantly in axons. Hyperphosphorylation of tau reduces the stability of microtubules, which may be a pathogenic mechanism in Alzheimer's disease. To understand the different effects between tau and glycogen synthase kinase 3beta (GSK-3beta) phosphorylated tau on the organization and stability of microtubules, we performed transfection studies on 3T3 cells using EGFP-tau (Enhanced Green Fluorescence Protein-tau) and GSK-3beta to quantify the stability of microtubules. Laser confocal microscope observation revealed that thick and thin microtubule bundles could be induced by tau and GSK-3beta phosphorylated tau. The bundles appeared either to be relatively straight or to form a ring around the circumference of the cell. Both the thick and thin microtubule bundles were resistant to colchicine-induced dissociation, with thick bundles more resistant than thin bundles. The bundles induced by GSK-3beta phosphorylated tau were sensitive to colchicine, and could be reversed by the addition of LiCl, an inhibitor of GSK-3beta.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Sang H,Lu Z,Li Y,Ru B,Wang W,Chen Jdoi
10.1016/s0304-3940(01)02206-6keywords:
subject
Has Abstractpub_date
2001-10-26 00:00:00pages
141-4issue
3eissn
0304-3940issn
1872-7972pii
S0304394001022066journal_volume
312pub_type
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