Protein kinase C involvement in cell cycle modulation.
Bologna, Italy. In Biochem Soc Trans, 2014
In particular, the targets of PKCs resulted to be some of the key proteins involved in the cell cycle including cyclins, cyclin-dependent kinases (Cdks), Cip/Kip inhibitors and lamins.
Tools for controlling protein interactions using light.
Aurora, United States. In Curr Protoc Cell Biol, 2013
We provide detailed protocols for experiments using two dimerization systems we previously developed, CRY2/CIB and UVR8/UVR8, for use in controlling transcription, protein localization, and protein secretion using light.
[Interactions of proliferation and differentiation signaling pathways in myogenesis].
Warsaw, Poland. In Postepy Hig Med Dosw (online), 2013
At the molecular level, several key regulators of the cell cycle have been identified: cyclin-dependent kinases and their cyclins stimulate the cell cycle progress and its arrest is determined by the activity of cdk inhibitors (Cip/Kip and INK protein families) and pocket protein family: Rb, p107 and p130.
Optical control of mammalian endogenous transcription and epigenetic states.
Cambridge, United States. In Nature, 2013
Here we describe the development of light-inducible transcriptional effectors (LITEs), an optogenetic two-hybrid system integrating the customizable TALE DNA-binding domain with the light-sensitive cryptochrome 2 protein and its interacting partner CIB1 from Arabidopsis thaliana.
Rapid blue-light-mediated induction of protein interactions in living cells.
Durham, United States. In Nat Methods, 2010
Here we describe genetically encoded light-inducible protein-interaction modules based on Arabidopsis thaliana cryptochrome 2 and CIB1 that require no exogenous ligands and dimerize on blue-light exposure with subsecond time resolution and subcellular spatial resolution.
Separating the good and evil of cardiac growth by CIB1 and calcineurin.
Dallas, United States. In Cell Metab, 2010
Heineke et al. (2010) show that CIB1 strongly enhances calcineurin activation and cardiac hypertrophy upon pathological stress, likely by functioning as a scaffold protein that exposes calcineurin to the L-Type Ca(2+) channel and the sarcolemma.