A novel role for hGas7b in microtubular maintenance: possible implication in tau-associated pathology in Alzheimer disease.
Here, we report a novel role for hGas7b (human growth arrest specific protein 7b) in the regulation of microtubules. Using a bioinformatic approach, we studied the actin-binding protein hGas7b with a structural similarity to the WW domain of a peptidyl prolyl cis/trans isomerase, Pin1, that facilitates microtubule assembly. Thus, we have demonstrated that hGas7b binds Tau at the WW motif and that the hGas7b/Tau protein complex interacts with the microtubules, promoting tubulin polymerization. Tau, in turn, contributes to protein stability of hGas7b. Furthermore, we observed decreased levels of hGas7b in the brains from patients with Alzheimer disease. These results suggest an important role for hGas7b in microtubular maintenance and possible implication in Alzheimer disease.
Department of Molecular Enzymology, Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-8555, Japan.
Hirotada
H
Akiyama
Aina
A
Gotoh
Ryong-Woon
RW
Shin
Tomoe
T
Koga
Tsubasa
T
Ohashi
Wataru
W
Sakamoto
Akihiro
A
Harada
Hiroyuki
H
Arai
Akira
A
Sawa
Chiyoko
C
Uchida
Takafumi
T
Uchida
D000544:Alzheimer Disease / Q000378:metabolism*; D020816:Amino Acid Motifs; D000818:Animals; D001921:Brain / Q000378:metabolism; D019556:COS Cells; D002522:Chlorocebus aethiops; D019295:Computational Biology; D018076:DNA, Complementary / Q000378:metabolism; D030562:Databases, Protein; D006801:Humans; D051379:Mice; D008840:Microfilament Proteins / Q000096:biosynthesis / Q000502:physiology*; D008870:Microtubules / Q000378:metabolism*; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000502:physiology*; D014404:Tubulin / Q000737:chemistry; D016875:tau Proteins / Q000737:chemistry*
D018076:DNA, Complementary; C114909:GAS7 protein, human; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins; D014404:Tubulin; D016875:tau Proteins