Title

The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.

Journal

The Journal of cell biology

Volume

192

Issue

None

Pages

647-61

Date

2011-02-21

Authors

Gauthier-Kemper A | Brandt R | Sebö-Lemke Z | Weissmann C | Gerke V | Golovyashkina N | Heinisch JJ | Drewes G

The quantification of all immunoreactive bands revealed that the R406W mutation exhibits a decreased phosphorylation at T205, T212, and the PHF1 epitope (S396/S404; reductions of 40–65%) as compared with wt tau, whereas other sites were not affected or only slightly affected (T181, S199, S214, and S262).

The data suggest that tau’s membrane association causes retention of tau in the tip of neurites, which is compromised by the R406W mutation. Also, after BAPTA treatment, the difference in the retention of wt tau and R406W tau was abolished (Fig. 9 D), which again suggests that tau trapping is caused by an interaction with AnxA2 at the membrane.

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