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A ubiquitin-like system mediates protein lipidation
A new mode of protein lipidation is reported, in which Apg8 is covalently conjugated to phosphatidylethanolamine through an amide bond between the C-terminal glycine and the amino group of phosph atidyleanolamine, mediated by a ubiquitination-like system.
Involvement of linear polyubiquitylation of NEMO in NF-κB activation
Results indicate that LUBAC is involved in the physiological regulation of the canonical NF-κB activation pathway through linear polyubiquitylation of NEMO.
Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
Cbp is revealed as a new component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs, involved in the membrane localization of Csk and in the Csk-mediated inhibition of c-Src.
Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion.
The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy*
Results indicate that the Atg12-Atg5 conjugate is a ubiquitin-protein ligase (E3)-like enzyme for Atg8-PE conjugation reaction, distinctively promoting protein-lipid conjugations.
A sequential program of dual phosphorylation of KaiC as a basis for circadian rhythm in cyanobacteria
Double phosphorylation converted KaiC from an autokinase to an autophosphatase, whereas complete dephosphorylation had the opposite effect, and these mechanisms serve as the basis for cyanobacterial circadian rhythm generation.
Structure and functional analysis of a marine bacterial carotenoid biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at the gene level
The astaxanthin biosynthetic pathway is proposed for the first time at the level of the biosynthesis genes because of the low substrate specificity of the crt genes.
Role of KaiC phosphorylation in the circadian clock system of Synechococcus elongatus PCC 7942.
- T. Nishiwaki, Y. Satomi, T. Kondo
- BiologyProceedings of the National Academy of Sciences…
- 21 September 2004
The results suggest that KaiC phosphorylation regulates its transcriptional repression activity by controlling its binding affinity for other clock proteins.
Roles of CLOCK Phosphorylation in Suppression of E-Box-Dependent Transcription
- H. Yoshitane, T. Takao, Y. Satomi, Ngoc-Hien Du, T. Okano, Y. Fukada
- Biology, ChemistryMolecular and Cellular Biology
- 4 May 2009
It is found that the CLOCK protein is kept mostly in the phosphorylated form throughout the day and is partly hyperphosphorylated in the suppression phase of E-box-dependent transcription in the mouse liver and NIH 3T3 cells.
Three Maize Leaf Ferredoxin:NADPH Oxidoreductases Vary in Subchloroplast Location, Expression, and Interaction with Ferredoxin1[w]
A comparison of LFNR transcripts in leaves of plants grown on variable nitrogen regimes revealed that LFNR1 and LFNR2 transcripts are relatively more abundant under conditions of high demand for NADPH, described in terms of the functional differentiation of maize LFNR isoenzymes.