Microtubule-binding domain of tau proteins.
نویسندگان
چکیده
منابع مشابه
The proline-rich domain and the microtubule binding domain of protein tau acting as RNA binding domains.
Neuronal tau, through its proline-rich domain and the microtubule binding domain, binds to RNA non-sequence-specifically via electrostatic interaction. This binding inhibits the activity of tau. Tau and RNA were also found to co-localize in SH-SY5Y cells suggesting that RNA has opportunities to interact with tau in cells.
متن کاملConformational transition state is responsible for assembly of microtubule-binding domain of tau protein.
In the brains of Alzheimer's disease patients, the tau protein dissociates from the axonal microtubule and abnormally aggregates to form a paired helical filament (PHF). One of the priorities in Alzheimer research is to clarify the mechanism of PHF formation. Although several reports on the regulation of tau assembly have been published, it is not yet clear whether in vivo PHFs are composed of ...
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Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer's disease (AD) and related tauopathies. Mass spectrometry studies indicate that tau acetylation sites cluster within the microtubule-binding region (MTBR), a region that is highly conserved among tau, MAP2, and MAP4 family members, implying that acetylation could represent a c...
متن کاملMicrotubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain.
We have analyzed the in vitro phosphorylation of tau protein by Ca2+/calmodulin-dependent protein kinase, casein kinase II, and proline-directed serine/threonine protein kinase. These kinases phosphorylate tau protein in sites localized in different regions of the molecule, as determined by peptide mapping analyses. Focusing on the phosphorylation of tau by protein kinase C, it was calculated a...
متن کاملMAP2c, but Not Tau, Binds and Bundles F-Actin via Its Microtubule Binding Domain
BACKGROUND MAP2 and tau are abundant microtubule-associated proteins (MAPs) in neurons. The development of neuronal dendrites and axons requires a dynamic interaction between microtubules and actin filaments. MAPs represent good candidates to mediate such interactions. Although MAP2c and tau have similar, well-characterized microtubule binding activities, their actin interaction is poorly under...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)68555-2