Talk:Trk receptor

A fact from Trk receptor appeared on Wikipedia's Main Page in the Did you know column on 2 December 2007. The text of the entry was as follows:

Did you know... that the first Trk receptor, which regulates synaptic strength and plasticity in neurons, was originally identified as part of a fusion gene with the cytoskeletal protein tropomyosin, forming an oncogene in colon and thyroid cancers?

A record of the entry may be seen at Wikipedia:Recent additions/2007/December.

Wikipedia

Molecular Biology: MCB

	This article is within the scope of WikiProject Molecular Biology, a collaborative effort to improve the coverage of Molecular Biology on Wikipedia. If you would like to participate, please visit the project page, where you can join the discussion and see a list of open tasks.Molecular BiologyWikipedia:WikiProject Molecular BiologyTemplate:WikiProject Molecular BiologyMolecular Biology articles
???	This article has not yet received a rating on the importance scale.
	This article is supported by the Molecular and Cell Biology task force (assessed as Low-importance).

Question

How do I add another reference to the list? (Thats for citation number 5) It gave me error when I did it

Responded on your talk page. --Alfadog (talk) 02:26, 28 November 2007 (UTC)[reply]

Origin of the Trk name

Hi, I've never changed anything on here, nor really know what I'm doing at the moment. Please be kind. Anyway, the Trk receptors are "tropomyosin-related kinases". I'm not sure how tropomyosin-receptor-kinase got into the article, since the reference cited goes with '-related'. Cheers, had to get that off my chest 84.201.140.75 (talk) 18:47, 21 April 2008 (UTC)[reply]

Del section from single paper

The following was removed. It is an explanation of the tests by which the conclusions summarized in the section above were reached. A bit of it is incoherent, some of which I edited before moving. It all comes from a single paper and is too specialized for this page.

"

TrkA and TrkB receptors activity are ligand-dependent

To test if TrkA and TrkB receptors activity are ligand-dependent, the receptors are treated with NGF and BDNF correspondingly.^[1] In vivo, the activity of these receptors is regulated by ubiquitination, the process in which protein undergoes modification by attachment of ubiquitin monomers.^[1] These molecules usually have main function of labeling proteins for proteasomal degradation.^[1] After being activated, Trk receptors may undergo endocytosis and will be either recycled or degraded.^[1] Two types of cells were used to test the protocol, PC12 cells and E16 mouse cortices.^[1] An E16 mouse cortex was used in conjunction with BDNF, since it expresses abundant TrkB and lesser p75NTR.^[1] On the other hands, PC12 cells were treated with NGF, since it expresses more TrkA and p75NTR but not TrkB and TrkC.^[1] The treated receptors were then immunoprecipitated and immunoblotted to be analyzed.^[1] The result shows that TrkB phosphotyrosine (activated TrkB) content increased rapidly with the presence of BDNF compared with control (absence of BDNF) whereas TrkA phosphotyrosine content increased modestly when treated with NGF.^[1]

p75NTR reduces Trk ubiquitination

To test if p75NTR reduces Trk ubiquitination, HEK293 (human embryonic kidney 293 cells) were co-tranfected with plasmids encoding TrkA and Myc-tagged ubiquitin with the presence and absence of plasmid encoding p75NTR.^[1] When treated with their corresponding neurotrophins, lower levels of ubiquitinated TrkA and TrkB are present in presence of p75NTR.^[1] Vice versa, in the absence of p75NTR, ubiquitination content increases significantly.^[1]

p75NTR delays Trk receptor internalization

To test the hypothesis, HEK93 cells were subjected to biotinylation with the presence and absence of p75NTR.^[1] Each samples were taken at different time points (0, 2, 5, and 15 mins), immunoblotted, and screened for the level of tyrosine-phosphorylated molecules.^[1] The result shows increases in the level of tyrosine-phosphorylated molecules with the presence of p75NTR.^[1] In absence of p75NTR, tyrosine-phosphorylated level fell below detection limit in 5 min.^[1] The biotinylated protein complexes were lysed to show both tyrosine-phosphorylated molecules in the surface and those that been internalized.^[1] "

173.25.54.191 (talk) 22:38, 8 December 2013 (UTC)[reply]

References

^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m ⁿ ^o ^p ^q Makkerh, J. P., Ceni, C., Auld, D. S., Vaillancourt, F., Dorval, G., Barker, P. A. (2005). p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation. EMBO Rep 6, 936–941.[Medline].

Propose to add larotrectinib, as a trk inhibitor already submitted for approval to fda

http://www.investor.bayer.com/en/nc/news/investor-news/investor-news/bayer-announces-initiation-of-rolling-submission-of-new-drug-application-in-the-us-for-larotrectin/ Wowbagger2 (talk) 22:55, 7 January 2018 (UTC)[reply]

[Makkerhl-1] ^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m ⁿ ^o ^p ^q Makkerh, J. P., Ceni, C., Auld, D. S., Vaillancourt, F., Dorval, G., Barker, P. A. (2005). p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation. EMBO Rep 6, 936–941.[Medline].

[1]