Talk:Tau protein

message: It's the WW domain of the Pin1 protein with a small peptide fragment of tau (14 residues out of ~600 residues)total. The figure is pretty misleading as is and should be deleted. In the meantime I am editing the caption to reflect this
--Biophysik (talk) 19:58, 8 June 2013 (UTC)
thread_title: Structure is not tau

message: I am an average person that can not understand most of this material. What I do understand is that mice have shown us that tau protiens may increase our tendency towards Alzheimers.
Is this in a particular food that I could avoid? 
Heinv 00:09, 4 May 2007 (UTC)
replies: text: Tau is a normal protein found within everyone's brain, so its not something you want to or can eliminate through diet. While it is clear that alterations to Tau such as mutations or chemical additions and changes in its regulation can cause neurodegenerative diseases, there is no definitive research about how you can change your diet to affect your chances of coming down with a neurodegenerative disease. 
128.111.227.19 17:12, 18 May 2007 (UTC)
thread_title:  Can we avoid tau proteins? 

message: Why wiki can suck.  Where is the art?  —Preceding unsigned comment added by 69.152.32.73 (talk) 07:52, 18 March 2011 (UTC)
thread_title:  Images & diagram needed. 

message: There are several paragraphs on how Tau proteins are phosphorylated. Because hyperphosphorylation leads to Tangles (Alzheimers), maybe it would make sense to mention how exactlt phosphorylation affects the Tau protein. — Preceding unsigned comment added by 137.43.182.167 (talk) 17:32, 23 October 2011 (UTC)
thread_title:  Function & Phosphorylation 

message: Content:
The article was not well organized but it had main points related to tau protein. Some materials are presented clearly and others were not understandable such as “genetic” and “interactions” section. This article did not cover the topic comprehensively, for example, in “clinical significance” section, they did not include enough details about the mechanism of tau release or tau toxicity. The quality of the evidence was accurate but I think it must include more details about phosphorylation effect on tau release. The article had references but couple of them were not reliable because they were from websites. I noticed that they mentioned “Tau hypothesis of Alzheimer's disease” which I think it is their assumption. Their content would be improved by adding some important information that were missing in this article, for example, specific details or image of tau isoforms. Also, adding information about how phosphorylation effect on tau release would be helpful.
 
Quality:
The article had an introduction but it is a little bit short which did not include enough information about tau. The introduction was clear and understandable but it did not summarize the main points. I would suggest including more background. The article had many headings and no subheadings. When I read the article, I noticed some important information was missing, for example, the difference between the role of tau in health and disease state. Also, in the “structure” section, they missed some essential points regarding domains. There were images included in this article and they were at appropriate place. I would suggest if they have image of tau protein structure or image of phosphorylated sites of tau. They included footnotes as well. The coverage was neutral and facts were emphasized. They had some reliable sources as they are peer-reviewed journals, but I noticed there were couple of sources are not reliable because they are from websites. — Preceding unsigned comment added by GhadirSindi (talk • contribs) 00:11, 25 October 2018 (UTC)
thread_title:  Article evaluation 

message: Changes that I made to the page:
1. changed the order of the content. I moved "genetics section" to be after "function section".
2.Function: 
Added information/citation:
“In addition to their microtubule stabilizing functions, MAPTs have also been found to recruit signaling proteins and regulation of microtubule-mediated transport [13].”
3.Genetics:
Citations were added (14,15).
4.Added new section:
Tau Mechanism
The accumulation of hyperphosphorylated tau in neurons will lead to the neurofibrillary degeneration.[25] The actual mechanism of how tau propagate from cell to another is not well identified. Also, other mechanisms including tau release and toxicity are unclear. As tau aggregates, it replaces tubulin which in turn enhance fibrilization of tau.[26] Several propagation methods have been proposed which occur by synaptic contact such as synaptic cell adhesion proteins and neuronal activity and other synaptic and non-synaptic mechanisms.[27]
Tau release
Tau involves in uptake and release process, which is known as seeding. Uptake of tau protein mechanism requires the presence of heparan sulfate proteoglycans at the cell surface which happen by macropinocytosis.[28] On the other hand, tau release depends on neuronal activity. Many factors influence tau release, for example, type of isoforms or MAPT mutations which change the extracellular level of tau.[29] According to Asai and his colleagues, spreading of tau protein occurs from entorhinal cortex to the hippocampal region in the early stages of the disease. They also suggested that microglia were also involved in the transport process and their actual rule is still unknown.[30]
Tau toxicity
Tau causes toxic effects through its accumulation inside cells. Many enzymes involved in toxicity mechanism such as PAR-1 kinase. This enzyme stimulates phosphorylation of serine 262 and 356, which in turn lead to activate other kinases (GSK-3 and Cdk5) that cause disease-associated phophoepitopes.[31] The degree of toxicity is affected by different factors such as the degree of microtubule binding.[32][33] Toxicity could also happen by NFTs which lead to cell death and cognitive decline.
5.Tau hypothesis of Alzheimer's disease
added information/citation
•	The stage of the disease determines NFTs phosphorylation. In AD, at least 19 amino acids are phosphorylated such as pre-NFTs phosphorylation occurs at serine 119, 202, and 409. While intra-NFT phosphorylation happens at serine 396 and threonine 231.[46]
•	Tau mutations have many consequences such as changing the expression level of tau isoforms or lead to MTs dysfunction.[47]
GhadirSindi (talk) 18:20, 28 November 2018 (UTC)
thread_title:  Editing assignment  

message: Seems to be an old name of hyperphosphorylated tau (as a monomer?) הסרפד (call me Hasirpad) 15:37, 24 May 2019 (UTC)
replies: text: Done. · • SUM1 • · (talk) 01:04, 27 January 2020 (UTC)
replies: text:  Thanks! הסרפד (call me Hasirpad) 21:27, 29 January 2020 (UTC)
thread_title:  Proposed merge with [[A68 protein]]