Technion – Israel Institute of Technology

About: Technion – Israel Institute of Technology is a education organization based out in Haifa, Israel. It is known for research contribution in the topics: Population & Upper and lower bounds. The organization has 31714 authors who have published 79377 publications receiving 2603976 citations. The organization is also known as: Technion Israel Institute of Technology & Ṭekhniyon, Makhon ṭekhnologi le-Yiśraʼel.

Spatial solitons in photorefractive media.

Abstract: We show that photorefractive media can support a new type of spatial soliton, in which the diffraction is balanced by the self-scattering (two-wave mixing) of the beam spatial frequency components. This photorefractive soliton possessses some unique properties, such as independence of the absolute light intensity, and can experience absorption (or gain) with no change in its transverse structure.

Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation

Abstract: The cellular abundance of the cyclin-dependent kinase (Cdk) inhibitor p27 is regulated by the ubiquitin–proteasome system. Activation of p27 degradation is seen in proliferating cells and in many types of aggressive human carcinomas. p27 can be phosphorylated on threonine 187 by Cdks, and cyclin E/Cdk2 overexpression can stimulate the degradation of wild-type p27, but not of a threonine 187-to-alanine p27 mutant [p27(T187A)]. However, whether threonine 187 phosphorylation stimulates p27 degradation through the ubiquitin–proteasome system or an alternative pathway is still not known. Here, we demonstrate that p27 ubiquitination (as assayed in vivo and in an in vitro reconstituted system) is cell-cycle regulated and that Cdk activity is required for the in vitro ubiquitination of p27. Furthermore, ubiquitination of wild-type p27, but not of p27(T187A), can occur in G1-enriched extracts only upon addition of cyclin E/Cdk2 or cyclin A/Cdk2. Using a phosphothreonine 187 site-specific antibody for p27, we show that threonine 187 phosphorylation of p27 is also cell-cycle dependent, being present in proliferating cells but undetectable in G1 cells. Finally, we show that in addition to threonine 187 phosphorylation, efficient p27 ubiquitination requires formation of a trimeric complex with the cyclin and Cdk subunits. In fact, cyclin B/Cdk1 which can phosphorylate p27 efficiently, but cannot form a stable complex with it, is unable to stimulate p27 ubiquitination by G1 extracts. Furthermore, another p27 mutant [p27(CK−)] that can be phosphorylated by cyclin E/Cdk2 but cannot bind this kinase complex, is refractory to ubiquitination. Thus throughout the cell cycle, both phosphorylation and trimeric complex formation act as signals for the ubiquitination of a Cdk inhibitor.