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• W1999605091 abstract "Rapid progress in analytical and synthetic methods has made possible the identification of multiple modifications that occur at different times and in different locations in the cell. The three minireviews in this series were derived from presentations given at the 16th Methods in Protein Structure Analysis Conference (MPSA2006) which took place in Lille, France, 28 August to 2 September, 2006 (see http://www.iapsap.bnl.gov). Each of the modifications discussed in these minireviews plays crucial roles in determining the functions of the proteins in which they occur. The focus of the first minireview by Nadolski and Linder is S-palmitoylation, a common and reversible lipid modification that occurs on the cytoplasmic leaflet of membranes. This modification influences the association of proteins with membranes, protein trafficking and protein stability. Interestingly, the regulation of palmitoylation is quite unique. Two classes of enzymes, acyltransferases and acylthioesterases, fine tune the degree of palmitoylation and depalmitoylation either constitutively or in response to different signals. The authors briefly discuss the sequence motifs for palmitoylation and the role that enzymes play in the transfer of palmitate from palmitoyl-CoA to a protein substrate. Genetic screens in yeast, followed by homology searches in mammalian genomes, have uncovered a family of enzymes of both physiological and pathophysiological importance. Future studies should allow the development of inhibitors with potential therapeutic applications. Protein phosphorylation on serine or threonine residues preceding proline (Ser/Thr-Pro) plays an important role in regulating various cellular processes. Further, proline is important for determining protein structure because it can adopt both cis or trans configurations, and the addition of a phosphate group before the proline can favor one configuration state over the other. In the second minireview, Lippens and colleagues report on studies examining the activity of Pin1, a prolyl cis/trans isomerase that regulates a number of proteins implicated in cell-cycle progression and human diseases. Although the enzymatic activity of Pin1 toward short peptides containing the phospho-Ser/Thr-Pro motif has been well documented, the activity toward natively unstructured regions of polypeptides with minor populations of the cis conformer of the phospho-Ser/Thr-Pro bond remains to be fully characterized. The authors describe the current status of knowledge of Pin1 activity on native polypeptides and suggest opportunities that may lead to a fuller understanding of Pin1's in vivo activity. The third minireview by Hatahet and Ruddock examines an enzyme important for protein folding. Protein disulfide isomerase (PDI) catalyzes protein folding through disulfide bond formation in secreted proteins. Native disulfide bond formation is dependent not only on PDI but also on its homologs, a combination of catalytically active and inactive thioredoxin domains. However, the contribution of PDI to the formation of native disulfides versus reduction/rearrangement of non-native disulfides is not clear. The minireview focuses on the interactions of the human PDI-family members with substrates, the characterization of their substrate binding sites and the determination of their endogenous substrates in vivo. The authors discuss both the ability of PDIs to act as chaperones and different ways of examining the interaction between PDI-family members and their substrates in vivo without cross-linkers. The latter methods are critical for our understanding of native disulfide bond formation." @default.
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• W1999605091 date "2007-09-24" @default.
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• W1999605091 title "Introduction: Post-translational modifications - S-palmitoylation, proline isomerization, disulfide bond isomerization" @default.
• W1999605091 doi "https://doi.org/10.1111/j.1742-4658.2007.06055.x" @default.
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