TY - JOUR
T1 - Lipin 2 binds phosphatidic acid by the electrostatic hydrogen bond switch mechanism independent of phosphorylation
AU - Eaton, James M.
AU - Takkellapati, Sankeerth
AU - Lawrence, Robert T.
AU - McQueeney, Kelley E.
AU - Boroda, Salome
AU - Mullins, Garrett R.
AU - Sherwood, Samantha G.
AU - Finck, Brian N.
AU - Villén, Judit
AU - Harris, Thurl E.
PY - 2014/6/27
Y1 - 2014/6/27
N2 - Background: Lipin 2 is a phosphatidic acid phosphatase (PAP) responsible for DAG formation at the ER membrane during lipogenesis. Results: A combination of biochemical approaches is used to characterize lipin 2 phosphatase activity and regulation. Conclusion: The electrostatic charge of PA regulates activity, but phosphorylation does not. Significance: These findings demonstrate differential regulation of PAP activity within the lipin family.
AB - Background: Lipin 2 is a phosphatidic acid phosphatase (PAP) responsible for DAG formation at the ER membrane during lipogenesis. Results: A combination of biochemical approaches is used to characterize lipin 2 phosphatase activity and regulation. Conclusion: The electrostatic charge of PA regulates activity, but phosphorylation does not. Significance: These findings demonstrate differential regulation of PAP activity within the lipin family.
UR - https://www.scopus.com/pages/publications/84903533455
U2 - 10.1074/jbc.M114.547604
DO - 10.1074/jbc.M114.547604
M3 - Article
C2 - 24811178
AN - SCOPUS:84903533455
SN - 0021-9258
VL - 289
SP - 18055
EP - 18066
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 26
ER -