Interaction between an intraluminal loop peptide of the inositol 1,4,5-trisphosphate receptor and the near N-terminal peptide of chromogranin A.
The near N-terminal region of chromogranin A (CGA) has been shown to be the secretory vesicle membrane binding region, and tetrameric chromogranin A has been demonstrated to bind four molecules of an intraluminal loop peptide of the inositol 1,4,5-trisphosphate (IP3) receptor. It was therefore necessary to determine whether the conserved near N-terminal region of CGA interacts with the intraluminal loop region of the IP3 receptor. In the present study, we found that the proposed anchor region of CGA, the conserved near N-terminal region, does indeed interact with the intraluminal loop region of the IP3 receptor at the intravesicular pH of 5.5, further strengthening the case for the potential interaction between tetrameric chromogranins and tetrameric IP3 receptors in the cell.
Yoo
S H
SH
Secretory Granule Research Group, Biomedical Research Center, Korea Advanced Institute of Science and Technology, Daejon, South Korea. shyoo@cais.kaist.ac.kr
Lewis
M S
MS
D015220:Calcium Channels / Q000737:chemistry / Q000378:metabolism*; D053379:Chromogranin A; D002864:Chromogranins / Q000737:chemistry / Q000378:metabolism*; D053496:Inositol 1,4,5-Trisphosphate Receptors; D008956:Models, Chemical; D011487:Protein Conformation; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000378:metabolism*
D015220:Calcium Channels; D053379:Chromogranin A; D002864:Chromogranins; D053496:Inositol 1,4,5-Trisphosphate Receptors; D018160:Receptors, Cytoplasmic and Nuclear