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. Author manuscript; available in PMC: 2012 May 12.
Published in final edited form as: Neuron. 2011 May 12;70(3):410–426. doi: 10.1016/j.neuron.2011.04.009

Figure 1. Tau Structure and Function.

Figure 1

Tau is an intrinsically disordered protein that can be alternatively spliced at N terminal exons (N1, 2) and the microtubule repeat domains (R). The domains of tau bind many different types of molecules, suggesting a central role in signaling pathways and cytoskeletal organization. The diversity of tau binding partners is highlighted in Table 1. N-term, N-terminus; C-term, C-terminus; SH3, protein SH3 domain