Talk:Retinoblastoma protein

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This

This article is a mess and it is difficult to even figure out how it came to be this way. When I go to the history for the article, the first entry (20:33, 17 October 2005) looks like it was thrown together from several sources. Ug. --JWSchmidt 01:11, 17 June 2006 (UTC)[reply]

It looks like the old reference list was truncated at some point....I hope I fixed it. I also added a few additional references, links, etc. --JWSchmidt 03:57, 17 June 2006 (UTC)[reply]

Rb gene was the first tumor suppressor discovered. it was described in context of retinoblastoma and Knudson's two hit hypothesis

Editing this article

This pRb article is consise but very narrow. It needs broadening to encompass the wealth of research on pRb and its distinct features. I will intergrate some chapters into this document and include relevent references. I'll post it in a few days for peer review and wikification.

Mutations in Rb

Does anyone know how mutations in either Rb or other proteins in the cyclin/Cdk pathway or p16 confer constitutive hyperphosphorylation of Rb? I could imagine only loss of p16 or a mutated inactive form of Rb could cause this constitutive phosphorylation, but cannot understand how mutations in the Rb gene itself confer this added capability to be phosphorylated.

--Nevermind, mutations that are involved in the pathogenesis of retinoblastoma are not limited to but include mutations in the entire signaling pathway. Yet neither the RB1 nor the retinoblastoma article makes mention of frequently mutated domains in any of these proteins. I was confused (as demonstrated above) even to how mutations in Rb effect E2F transcription. Indeed, mutations in Rb preclude its sequestration of E2F in the "core pathway." However, the entire pathway is important and should be expanded upon in either this article or the retinoblastoma article. At the very least, viewers should understand that most mutations of Rb prevent its binding to E2F and prevent the subsequent transcription of genes related to progression of the cell cycle. I do not have enough experience to write a well-delineated article on here -- however, I direct the writer or the viewer pre-update to this good review article on Rb pathogenesis. Sellers and Kaelin 15 (11): 3301. (1997)

--Can someone change the importance of this article for update. This article is very incomplete outside of its important history in the beginnings of cancer research. I do not understand how such an important protein in cancer research is ranked so low. To me, when you hear about cancer in its surrounding boundless field of research, you hear about p53, then you hear about Rb. I think this article deserves some work based on the incredible amount of information I was able to garner from reading simply one review article that is not anywhere mentioned on either the gene/protein/cancer page for Rb.—Preceding unsigned comment added by 129.98.121.182 (talk) 15:08, 15 November 2009 (UTC)[reply]

Hey, thanks for the thoughts. Feel free to add any info to the article that you think is missing, using references from journals and books. (The review article sounds like a good reference). You can also change the importance rating yourself by changing the template at the top of the page, but maybe we should wait around to hear if anyone objects (I doubt anyone will). Let me know if you need any help editing or whatnot. delldot ∇. 20:49, 15 November 2009 (UTC)[reply]

Wrong arrow in flow chart

The arrow in the flow chart indicating that RB stimulates E2F is wrong, as it inhibits E2F by means of binding/blocking. By blocking E2F, RB stalls a cell at the G1 phase until it is ready for the S-phase. The cell will signal that it is ready by CDK4/Cyclin D[[1]], which will phosphorylate RB and thereby inhibit RB.

http://wiki.riteme.site/wiki/File:Signal_transduction_v1.png

This image should be corrected as it is used in many articles. — Preceding unsigned comment added by 82.136.233.58 (talk) 21:00, 5 September 2013 (UTC)[reply]

Phosphorylation and pRb

The text in section "Activation and inactivation" states: "Rb is phosphorylated to pRb...". I am pretty sure that "pRb" is not a specific name for the phosphorylated form, but that the "p" stands for "protein" (ie the protein encoded by the Rb gene). Anyone disagree? --Wdanbae (talk) 14:15, 2 July 2014 (UTC)[reply]

Re: naming of pRb

In response to the above note about Rb 'becoming' pRb when it's phosphorylated - I agree that this is probably incorrect. Given that it hasn't been cited, and is commonly understood to just refer to it being the protein product of the Rb gene (compare to other protein names in cancer biology: p53, p21, etc.), I have corrected this in the article. IsaacWoodsMedicine (talk) 16:02, 9 May 2021 (UTC)[reply]