The PAR2 signal peptide prevents premature receptor cleavage and activation
نویسندگان
چکیده
منابع مشابه
SPEPlip: the detection of signal peptide and lipoprotein cleavage sites
SUMMARY SPEPlip is a neural network-based method, trained and tested on a set of experimentally derived signal peptides from eukaryotes and prokaryotes. SPEPlip identifies the presence of sorting signals and predicts their cleavage sites. The accuracy in cross-validation is similar to that of other available programs: the rate of false positives is 4 and 6%, for prokaryotes and eukaryotes respe...
متن کاملSequences beyond the cleavage site influence signal peptide function.
The earliest events in protein secretion include targeting to and translocation across the endoplasmic reticulum membrane. To dissect the mechanism by which signal sequences mediate translocation in eukaryotes, we are examining the behavior of fusion proteins and deletion mutants in cell-free systems. We demonstrate that the protein domain being translocated can have profound impact on the effi...
متن کاملSignal peptide cleavage in the E . coli membrane
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, B.C. Canada V6T 1Z3 Abstract Our laboratory uses x-ray crystallography and other structural biology techniques in the analysis of bacterial membrane proteins and membrane protein complexes. We are particularly interested in bacterial protein secretion machinery, including the Sec-dependent translocation...
متن کاملA Gas Carboxyl-Terminal Peptide Prevents Gs Activation by the A2A Adenosine Receptor
The molecular mechanisms of interaction between Gs and the A2A adenosine receptor were investigated using synthetic peptides corresponding to various segments of the Gas carboxyl terminus. Synthetic peptides were tested for their ability to modulate binding of a selective radiolabeled agonist, [H]2-[4-(2-carboxyethyl)phenylethylamino]-59-N-ethylcarboxamidoadenosine ([H]CGS21680), to A2A adenosi...
متن کاملCathepsin B cleavage of the trypsinogen activation peptide
BACKGROUND Cathepsin B is thought to play a central role in intrapancreatic trypsinogen activation and the onset of pancreatitis. A recent investigation of the cathepsin B mediated activability of wildtype trypsinogen and their mutations N29I, N29T and R122H, which are associated to hereditary pancreatitis, revealed no differences. This action seems to be restricted to the K23-I24 peptide bond,...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLOS ONE
سال: 2020
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0222685