Identification of a sorting signal for the regulated secretory pathway at the N-terminus of pro-opiomelanocortin
作者： D.R. Cool , Y. Peng Loh
DOI: 10.1016/0300-9084(94)90156-2
关键词: Chloramphenicol acetyltransferase 、 Prohormone 、 N-terminus 、 Amino acid 、 Peptide sequence 、 Biology 、 Signal transduction 、 Wild type 、 Biochemistry 、 Secretion
摘要: The N-terminal 26 amino acids of the prohormone pro-opiomelanocortin (POMC) were investigated to determine whether this region has capacity act as a sorting signal for regulated secretory pathway. Constructs made using 101, 50, or 10 POMC fused chloramphenicol acetyltransferase (CAT) reporter protein and expressed in AtT20 cells show that at least first required sort CAT Full length was mutated by deleting 2-26 from region. Analysis Neuro-2a expressing mutation compared wild type indicated these contain information essential results presented here suggest presence conformation-dependent responsible
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