TY - JOUR
T1 - How a helix imposes palmitoylation of a membrane protein
T2 - What one can learn from NCX
AU - Khananshvili, Daniel
N1 - Publisher Copyright:
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2017/6/23
Y1 - 2017/6/23
N2 - Palmitoylation is a critical post-translational modification that anchors proteins to, and regulates transport across, the lipid bilayer. Palmitoylation enzymes have been assumed to select their substrates based on a protein’s primary sequence, but a consensus sequence has been slow to emerge. A study of the sodium/calcium exchanger now suggests that secondary structure may hold the key to understanding the determinants of this modification.
AB - Palmitoylation is a critical post-translational modification that anchors proteins to, and regulates transport across, the lipid bilayer. Palmitoylation enzymes have been assumed to select their substrates based on a protein’s primary sequence, but a consensus sequence has been slow to emerge. A study of the sodium/calcium exchanger now suggests that secondary structure may hold the key to understanding the determinants of this modification.
UR - http://www.scopus.com/inward/record.url?scp=85021640037&partnerID=8YFLogxK
U2 - 10.1074/jbc.H116.773945
DO - 10.1074/jbc.H116.773945
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AN - SCOPUS:85021640037
SN - 0021-9258
VL - 292
SP - 10753
EP - 10754
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 25
ER -