Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
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References
LHC constraints on W ', Z ' that couple mainly to third generation fermions
EUROPEAN PHYSICAL JOURNAL C
Authors: Hayreter, Alper; He, Xiao-Gang; Valencia, German
We use the results of CMS and ATLAS searches for resonances that decay to tau nu or tb and tau(+)tau(-) or t (t) over bar final states to constrain the parameters of non-universal W' and Z' gauge bosons that couple preferentially to the third generation. For the former we consider production from c (b) over bar annihilation and find very weak constraints on the strength of the interaction and only for themass range between 800 and 1100 GeV from the pp -> tau(h)p(T)(miss) channel. The constraints on the latter are much stronger and arise from both t (t) over bar and tau(+)tau(-) production. Treated separately, we find that the weak constraints on the W' still permit an explanation of the R(D-(star)) anomalies with a light sterile neutrino whereas the stronger constraints on the Z' exclude significant light sterile neutrino contributions to the K -> pi nu(nu) over bar rates. Within specific models the masses of W' and Z' are of course related and we briefly discuss the consequences.
Key Physicochemical and Biological Factors of the Phase Behavior of Tau
CHEM
Authors: Nam, Geewoo; Lin, Yuxi; Lim, Mi Hee; Lee, Young-Ho
Recent findings have garnered a substantial amount of attention toward tau based on its pathological contribution to neurodegenerative diseases, such as Alzheimer's disease (AD). Studies investigating the structure and aggregation of tau under various in vitro and in vivo conditions have revealed its intrinsically disordered structures and amyloidogenesis process. The aggregation behavior of tau is strongly dependent on the experimental conditions due to the high sensitivity of both the soluble tau conformations and the amyloid nucleation process toward its surrounding environments. Herein, we review and discuss (1) the effects of different physicochemical and biological factors as well as intermolecular interactions with various molecular chaperones on tau aggregation, (2) context-dependent liquid-liquid phase separation of tau and its amyloidogenic transformation, and (3) the utility of the phase diagram in comprehending the phase transition and separation of proteins.
COA
Publication 
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