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Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis.
The duration of FGFR1 signaling seems to be tightly regulated by receptor ubiquitinations and subsequent sorting to the lysosomes for degradation, indicating that ubiquitination of the receptor is not required for endocytosis.
Two nuclear localization signals required for transport from the cytosol to the nucleus of externally added FGF-1 translocated into cells.
Evidence is provided that FGF-1 contains a second putative NLS (NLS2), which is located near the C-terminus, which is a bipartite NLS consisting of two clusters of lysines separated by a spacer of 10 amino acids, indicating that it can act as an NLS in the living cell.
Translocation of FGF-1 and FGF-2 across vesicular membranes occurs during G1-phase by a common mechanism.
The data indicate that translocation occurs from intracellular vesicles containing proton pumps and that an electrical potential across the vesicle membrane is required.
Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1.
Evidence is presented that phosphorylation of FGF-1 occurs in the nucleus by protein kinase C (PKC)delta, and that nucleocytoplasmic trafficking of the phosphorylated growth factor is likely to play a role in the activity of internalized F GF-1.
Protein lysine methylation by seven-β-strand methyltransferases.
A number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins.
Vesicle transmembrane potential is required for translocation to the cytosol of externally added FGF‐1
The data indicate that translocation of FGF‐1 to cytosol occurs from the lumen of intracellular vesicles possessing vacuolar proton pumps, and that a vesicular membrane potential is required.
Fluorescence study ofEscherichia coli cyclic AMP receptor protein
Time-resolved, steady-state fluorescence and fluorescence-detected circular dichroism (FDCD) have been used to resolve the fluorescence contributions of the two tryptophan residues, Trp-13 and
Identification and Characterization of a Novel Evolutionarily Conserved Lysine-specific Methyltransferase Targeting Eukaryotic Translation Elongation Factor 2 (eEF2)*
The present study establishes the function of the previously uncharacterized MTases FAM86A and Yjr129c, demonstrating that these enzymes introduce a functionally important lysine methylation in eEF2.
Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein.
The cAMP-mediated conformational and structural dynamics changes in the wild-type CRP were investigated using hydrogen-deuterium exchange and Fourier transform infrared spectroscopy to investigate the ability of cAMP to effect an increase in the dynamic motions of the DNA binding domain.
Kinetic Studies of cAMP-induced Allosteric Changes in Cyclic AMP Receptor Protein from Escherichia coli *
Stopped-flow fluorimetry was employed to study the kinetics of the conformational changes in CRP induced by cAMP binding to high and low affinity receptor sites, suggesting that conformational change precedes the formation of CRP-cAMP4 complex and results from displacement of equilibrium between two forms ofCRP- cAMP2.