Silicon Investor (SI) -- The First Internet Community

STOCKTALK

We've detected that you're using an ad content blocking browser plug-in or feature. Ads provide a critical source of revenue to the continued operation of Silicon Investor. We ask that you disable ad blocking while on Silicon Investor in the best interests of our community. If you are not using an ad blocker but are still receiving this message, make sure your browser's tracking protection is set to the 'standard' level.

Biotech / Medical : Rigel Pharmaceuticals, Inc. (RIGL) -- Ignore unavailable to you. Want to Upgrade?

To: tuck who wrote (253)	5/2/2005 6:14:21 AM
From: mopgcw	Read Replies (2) \| Respond to of 566

With MPM breaking up, I wonder what this will mean for RIGL (and others)..

To: tuck who wrote (253)	8/22/2007 2:22:06 PM
From: tuck	Respond to of 566

[Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme] >>J Biol Chem. 2007 Aug 20; [Epub ahead of print] Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme. Petroski MD, Zhou X, Dong G, Daniel-Issakani S, Payan DG, Huang J. Rigel Pharmaceuticals, South San Francisco, CA 94080. Protein modification with lysine 63 (K63)-linked ubiquitin chains has been implicated in the non-proteolytic regulation of signaling pathways. To understand the molecular mechanisms underlying this process, we have developed an in vitro system to examine the activity of the ubiquitin-conjugating enzyme UBC13-UEV1a with TRAF6 in which TRAF6 serves as both a ubiquitin ligase and substrate for modification. Although TRAF6 potently stimulates the activity of UBC13-UEV1a to synthesize ubiquitin chains, it is not appreciably ubiquitinated. We have determined that the presentation of K63 of ubiquitin by UEV1a effectively blocks TRAF6 modification. Based on our observations, we propose that the modification of proteins with K63-linked ubiquitin chains occurs through a UEV1a-independent substrate modification and UEV1a-dependent K63-linked ubiquitin chain synthesis mechanism.<< Parking another ligase related abstract that I don't have a clue about re: implications for drug development. Cheers, Tuck