Talk:Bcl-2 family

Latest comment: 7 years ago by Minus80 in topic Reorganization

Untitled

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Created as Apoptosis regulator proteins, Bcl-2 family

Merge with Bcl-2

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The Bcl-2 article seems to already have significant information about the Bcl-2 family as well as the specific Bcl-2 protein; this article doesn't appear to have much additional information so I believe a merge is in order. I originally suggested merging this into Bcl-2, but perhaps it'd be more appropriate to merge the portions of the Bcl-2 article dealing with the family into this article, and leave just a brief description of the family in the Bcl-2 article with a {{main article}} template directing to this article. I will update the merge templates accordingly in a moment.

In any case this page should be moved though, since the title is not appropriate. I will try to find out convention on naming of families of proteins and then move the page. GiftigerWunsch [TALK] 09:25, 6 June 2010 (UTC)Reply

To clarify, my proposition is to merge information from Bcl-2 relating to the Bcl-2 family, into this article (and also to move this article to Bcl-2 family) GiftigerWunsch [TALK] 09:46, 6 June 2010 (UTC)Reply
Thanks for pointing this out; I'd never used this particular template before. I've updated the template now. GiftigerWunsch [TALK] 10:05, 6 June 2010 (UTC)Reply

I did move some text over; please help with the merging, and remove the Move templates once it's done. --Magnus Manske (talk) 08:38, 13 August 2010 (UTC)Reply

Which is better?

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The text originaly read:

All anti-apoptotic proteins contain BH1 and BH2 domains, some of them contain an additional N-terminal BH4 domain (Bcl-2, Bcl-x(L), Bcl-w). On the other hand, all pro-apoptotic proteins contain a BH3 domain necessary for binding to other proteins of Bcl-2 family and crucial for their killing activity...

which was then changed to:

All anti-apoptotic proteins contain BH1 and BH2 domains, some of them contain an additional N-terminal BH4 domain (Bcl-2, Bcl-x(L), Bcl-w), which is never seen in pro-apoptotic proteins, except for Bcl-x(S). On the other hand, all pro-apoptotic proteins contain a BH3 domain (except for Bad) necessary for dimerization with other proteins of Bcl-2 family and crucial for their killing activity..

And then reverted back. Which version is more correct? —Preceding unsigned comment added by Abergabe (talkcontribs) 15:01, 2 July 2010 (UTC)Reply

I'd say neither; the second version adds a couple of details and a lot of confusion. I would rephrase the second version, but first it'd be best to get references to show that the added details are actually verifiable. GiftigerWunsch [TALK] 15:23, 2 July 2010 (UTC)Reply

I really couldn't say either way, but I reckoned it ought to be acknowledged and recorded so hopefuly it can give another editor some ideas :) Abergabe (talk) 15:42, 2 July 2010 (UTC)Reply

What is normal function of anti-apoptosis genes

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Article says "Many viruses have found a way of countering defensive apoptosis by encoding their own anti-apoptosis genes preventing their target-cells from dying too soon." but does not seem to say why non-viruses would express any anti-apoptosis genes. ? - Rod57 (talk) 11:54, 11 December 2015 (UTC)Reply

Reorganization

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I will move the Structure section before the Function section, as Function depends on Structure, and classification of various Bcl-2 family members are also based on structure. Currently it is unclear what the different members of the Bcl-2 family are, so I will summarize this and provide links to their individual pages under the Structure section as well. Minus80 (talk) 16:58, 17 January 2017 (UTC)Reply

There is also a lot of specific discussion on Bcl-xL but not sure why. Right now the article reads as if Bcl-xL is the most important or well-studied member when in fact most family members are known to have important roles in physiology and disease. Info specific to Bcl-xL will be merged to the Bcl-xL page or deleted, and the info which can be generalized will be generalized to the entire family. Minus80 (talk) 17:21, 17 January 2017 (UTC)Reply