Tau protein: Difference between revisions
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''' | Tau protein | ||
[[File:MAP2-tau_in_neurons.jpg|thumb|right|Microtubule-associated protein 2 (MAP2) and tau in neurons]] | |||
The '''tau protein''' is a [[microtubule-associated protein]] that is abundant in the [[central nervous system]]. It plays a critical role in stabilizing [[microtubules]], which are essential components of the [[cytoskeleton]] in [[neurons]]. Tau proteins are primarily found in [[neurons]] rather than [[non-neuronal cells]]. | |||
==Structure== | ==Structure== | ||
Tau proteins are | Tau proteins are encoded by the [[MAPT gene]] located on [[chromosome 17]]. The protein consists of multiple [[isoforms]] that arise from [[alternative splicing]] of the MAPT gene. These isoforms differ in the number of [[microtubule-binding domains]] they contain, which affects their ability to stabilize microtubules. | ||
==Function== | ==Function== | ||
Tau proteins are involved in | Tau proteins are involved in the assembly and stabilization of microtubules. They bind to the [[tubulin]] subunits of microtubules, promoting their polymerization and stability. This function is crucial for maintaining the structure and function of [[axons]] in neurons, facilitating [[axonal transport]] of [[organelles]], [[proteins]], and other cellular components. | ||
==Pathology== | |||
Tau proteins are implicated in several [[neurodegenerative diseases]], collectively known as [[tauopathies]]. In these conditions, tau proteins become abnormally [[phosphorylated]], leading to the formation of [[neurofibrillary tangles]] inside neurons. These tangles disrupt normal cellular function and are a hallmark of diseases such as [[Alzheimer's disease]], [[frontotemporal dementia]], and [[chronic traumatic encephalopathy]]. | |||
== | ===Alzheimer's Disease=== | ||
In [[Alzheimer's disease]], tau proteins undergo hyperphosphorylation, which reduces their ability to bind to microtubules. This results in the destabilization of the neuronal cytoskeleton and the formation of neurofibrillary tangles, contributing to neuronal death and cognitive decline. | |||
===Other Tauopathies=== | |||
[[ | Other tauopathies include [[Pick's disease]], [[progressive supranuclear palsy]], and [[corticobasal degeneration]]. Each of these conditions is characterized by the accumulation of abnormal tau protein aggregates in specific regions of the brain, leading to distinct clinical symptoms. | ||
[[ | |||
[[ | |||
==Research and Therapeutics== | |||
Research into tau proteins is ongoing, with efforts focused on understanding the mechanisms of tau aggregation and developing therapeutic strategies to prevent or reverse tau pathology. Potential approaches include the use of [[tau-targeting antibodies]], [[small molecules]] that inhibit tau aggregation, and [[gene therapy]] techniques to modulate tau expression. | |||
== | ==Related pages== | ||
* [[Microtubule]] | * [[Microtubule-associated protein]] | ||
* [[Neurofibrillary tangle]] | |||
* [[Alzheimer's disease]] | * [[Alzheimer's disease]] | ||
* [[ | * [[Neurodegenerative disease]] | ||
{{Neuroscience}} | |||
[[Category:Proteins]] | |||
[[Category:Neuroscience]] | |||
[[Category:Neurodegenerative disorders]] | |||
Latest revision as of 14:45, 22 February 2025
Tau protein
The tau protein is a microtubule-associated protein that is abundant in the central nervous system. It plays a critical role in stabilizing microtubules, which are essential components of the cytoskeleton in neurons. Tau proteins are primarily found in neurons rather than non-neuronal cells.
Structure[edit]
Tau proteins are encoded by the MAPT gene located on chromosome 17. The protein consists of multiple isoforms that arise from alternative splicing of the MAPT gene. These isoforms differ in the number of microtubule-binding domains they contain, which affects their ability to stabilize microtubules.
Function[edit]
Tau proteins are involved in the assembly and stabilization of microtubules. They bind to the tubulin subunits of microtubules, promoting their polymerization and stability. This function is crucial for maintaining the structure and function of axons in neurons, facilitating axonal transport of organelles, proteins, and other cellular components.
Pathology[edit]
Tau proteins are implicated in several neurodegenerative diseases, collectively known as tauopathies. In these conditions, tau proteins become abnormally phosphorylated, leading to the formation of neurofibrillary tangles inside neurons. These tangles disrupt normal cellular function and are a hallmark of diseases such as Alzheimer's disease, frontotemporal dementia, and chronic traumatic encephalopathy.
Alzheimer's Disease[edit]
In Alzheimer's disease, tau proteins undergo hyperphosphorylation, which reduces their ability to bind to microtubules. This results in the destabilization of the neuronal cytoskeleton and the formation of neurofibrillary tangles, contributing to neuronal death and cognitive decline.
Other Tauopathies[edit]
Other tauopathies include Pick's disease, progressive supranuclear palsy, and corticobasal degeneration. Each of these conditions is characterized by the accumulation of abnormal tau protein aggregates in specific regions of the brain, leading to distinct clinical symptoms.
Research and Therapeutics[edit]
Research into tau proteins is ongoing, with efforts focused on understanding the mechanisms of tau aggregation and developing therapeutic strategies to prevent or reverse tau pathology. Potential approaches include the use of tau-targeting antibodies, small molecules that inhibit tau aggregation, and gene therapy techniques to modulate tau expression.
Related pages[edit]
