p8 and prothymosin alpha: unity is strength.

Cell Cycle
Cédric MalicetJuan L Iovanna

Abstract

p8 and prothymosin alpha are two natively unstructured proteins with anti-apoptotic activity. We showed that their interaction results in the formation of a one-to-one heterodimer complex with stable structure. To test whether the heterodimer bears the function previously attributed to both proteins, we monitored the consequences on apoptosis of modulating in vitro the concentrations of both proteins. Overexpression was obtained by transfection of appropriate vectors and inhibition by using specific siRNAs. In all conditions inhibition of apoptosis correlated with the level of the partner with lowest concentration, demonstrating that the anti-apoptotic effect previously attributed to each proteins was in fact borne by the p8/ProTalpha complex, the two proteins, being individually inactive. These results show that the function attributed to a natively unfolded protein might actually belong to a multi-protein complex in which the protein of interest is engaged.

Citations

Dec 29, 2006·The Journal of Antibiotics·Tetsuro MorimuraFumio Sugawara
May 21, 2009·General and Comparative Endocrinology·Marina PriscoPiero Andreuccetti
Oct 11, 2012·Annals of the New York Academy of Sciences·Hiroshi UedaSebok Kumar Halder
Mar 29, 2019·The Journal of Clinical Investigation·Patricia Santofimia-CastañoJuan Iovanna
Nov 21, 2019·Cells·Patricia Santofimia-CastañoJuan Iovanna
Nov 2, 2019·Cellular and Molecular Life Sciences : CMLS·Patricia Santofimia-CastañoJuan Iovanna
Aug 4, 2009·Journal of Cellular Physiology·Meritxell GironellaJuan Lucio Iovanna
Nov 20, 2018·Scientific Reports·Patricia Santofimia-CastañoJuan Iovanna

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