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Membrane protein‐lipid hydrogen bonding: evidence from protein kinase C, diglyceride, and tumor promotors
Author(s) -
Brockerhoff Hans
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80559-2
Subject(s) - diacylglycerol kinase , chemistry , diglyceride , hydrogen bond , protein kinase c , protein kinase a , lipid bilayer , prkcq , biochemistry , membrane , biophysics , enzyme , stereochemistry , mitogen activated protein kinase kinase , organic chemistry , biology , molecule
Membrane‐bound proteins owe their retention and conformation in the lipid bilayer to hydrophobic peptide domains. Additional fixation, by protein‐lipid hydrogen bonding, has been suggested, and recent reports on protein kinase C activation by diacylglycerol (DG) provide an unambiguous model for such bonding. The sn ‐1,2‐diacylglycerol appears to donate a hydrogen bond from the sn ‐3 hydroxyl to the enzyme and to receive two hydrogen bonds, in the sn ‐1 and sn ‐2 ester CO groups, from the enzyme. This arrangement is confirmed in phorbol ester, a competitive inhibitor of DG for the kinase. This tumor promotor has a nearly identical spatial arrangement of hydrogen bond donor (9α‐OH) and acceptors (12 and 13 ester CO); so have two other tumor promotors, teleocidin and aplysiatoxin. There are reasons to believe that protein kinase C is not the only protein that is bound to membrane lipids by hydrogen bonding, and such bonding will have to be considered in membrane‐associated events such as fusion, cross‐membrane transport, or anesthesia.