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the ECF (enterleuking factor) and APC (anaphase promoting complex) are responsible for ubiquitylating CKIs (cycklin kinase inhibitors) growth factor-induced signalling in tumor cells ..

is their any other phosphorylation of Rb (retinoblastoma protein) which frees E2F (to act as a transricption factor) on any S-phase genes, leading to cell cycle entry, as well as p27 degradation? (by increasing transcription of SCF or any other means)

help appreciated!!

2007-01-22 07:16:50 · 2 answers · asked by Sea Bass 4 in Science & Mathematics Biology

2 answers

I think Yahoo Answers is the wrong place to go unless you're looking for this:

The ubiquitin-proteasome pathway regulates gene expression through protein degradation. Here we show that the F-box protein βTrCP, the receptor component of the SCF E3 ubiquitin ligase responsible for IκBα and β-catenin degradation, is colocalized in the nucleus with ATF4, a member of the ATF-CREB bZIP family of transcription factors, and controls its stability. Association between the two proteins depends on ATF4 phosphorylation and on ATF4 serine residue 219 present in the context of DSGXXXS, which is similar but not identical to the motif found in other substrates of βTrCP. ATF4 ubiquitination in HeLa cells is enhanced in the presence of βTrCP. The F-box-deleted βTrCP protein behaves as a negative transdominant mutant that inhibits ATF4 ubiquitination and degradation and, subsequently, enhances its activity in cyclic AMP-mediated transcription. ATF4 represents a novel substrate for the SCFβTrCP complex, which is the first mammalian E3 ubiquitin ligase identified so far for the control of the degradation of a bZIP transcription factor.

2007-01-22 07:25:53 · answer #1 · answered by Gretchen C 2 · 0 0

wow your question is way above the knowledge of the basic yahoo answers user, you must be very smart and intelligent

i agree though with the above answer

2007-01-24 06:11:17 · answer #2 · answered by Anonymous · 0 0

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