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{{Short description|A protein associated with microtubule stabilization and neurodegenerative diseases}}
Tau protein


'''Tau protein''' is a [[protein]] that plays a critical role in the stabilization of [[microtubules]] in [[neurons]]. It is predominantly found in the [[central nervous system]] and is associated with several [[neurodegenerative diseases]], collectively known as [[tauopathies]].
[[File:MAP2-tau_in_neurons.jpg|thumb|right|Microtubule-associated protein 2 (MAP2) and tau in neurons]]


==Structure and Function==
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]].
Tau protein is a member of the [[microtubule-associated proteins]] (MAPs) family. It is primarily expressed in neurons, where it binds to and stabilizes microtubules, which are essential components of the [[cytoskeleton]]. Microtubules are involved in maintaining cell shape, enabling intracellular transport, and facilitating cell division.


Tau protein is encoded by the [[MAPT gene]] located on [[chromosome 17]]. The protein undergoes alternative splicing, resulting in six isoforms in the adult human brain. These isoforms differ in the number of microtubule-binding repeats and the presence of N-terminal inserts, which influence their binding affinity to microtubules.
==Structure==
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.


==Role in Neurodegenerative Diseases==
==Function==
Tau protein is implicated in a group of neurodegenerative disorders known as tauopathies. The most well-known of these is [[Alzheimer's disease]], where abnormal hyperphosphorylation of tau leads to the formation of [[neurofibrillary tangles]] (NFTs). These tangles disrupt neuronal function and are a hallmark of the disease.
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.


Other tauopathies include:
==Pathology==
* [[Progressive supranuclear palsy]]
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]].
* [[Corticobasal degeneration]]
* [[Frontotemporal dementia with parkinsonism linked to chromosome 17]] (FTDP-17)


In these conditions, tau protein undergoes pathological changes, including hyperphosphorylation, truncation, and aggregation, leading to neuronal dysfunction and cell death.
===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.


==Pathophysiology==
===Other Tauopathies===
The pathophysiological mechanisms of tau-related neurodegeneration involve several processes:
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.


* '''Hyperphosphorylation''': Abnormal phosphorylation of tau reduces its affinity for microtubules, causing it to detach and aggregate into insoluble filaments.
==Research and Therapeutics==
* '''Aggregation''': Detached tau proteins aggregate into paired helical filaments (PHFs) and straight filaments, which form the core of neurofibrillary tangles.
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.
* '''Cellular Dysfunction''': The accumulation of tau aggregates disrupts cellular processes, including axonal transport, synaptic function, and neuronal communication.
 
==Research and Therapeutic Approaches==
Research into tau protein focuses on understanding its normal function, the mechanisms of its pathological transformation, and developing therapeutic strategies to prevent or reverse tau-related neurodegeneration.
 
Therapeutic approaches include:
* '''Tau-targeting drugs''': Small molecules or antibodies that inhibit tau aggregation or promote its clearance.
* '''Gene therapy''': Techniques to modulate tau expression or correct mutations in the MAPT gene.
* '''Phosphorylation inhibitors''': Compounds that prevent abnormal phosphorylation of tau.
 
==Images==
[[File:Tau_protein_structure.png|thumb|right|Diagram of tau protein structure showing microtubule-binding domains.]]
 
[[File:Neurofibrillary_tangles.png|thumb|left|Histological image of neurofibrillary tangles in Alzheimer's disease.]]


==Related pages==
==Related pages==
* [[Microtubule]]
* [[Microtubule-associated protein]]
* [[Neurofibrillary tangle]]
* [[Alzheimer's disease]]
* [[Neurodegenerative disease]]
* [[Neurodegenerative disease]]
* [[Alzheimer's disease]]
 
* [[Frontotemporal dementia]]
{{Neuroscience}}


[[Category:Proteins]]
[[Category:Proteins]]
[[Category:Neuroscience]]
[[Category:Neurodegenerative disorders]]
[[Category:Neurodegenerative disorders]]
[[Category:Tauopathies]]

Latest revision as of 14:45, 22 February 2025

Tau protein

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[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]