Phosphorylation of F1F0 ATPase delta-subunit is regulated by platelet-derived growth factor in mouse cortical neurons in vitro.
The delta subunit of F1F0 ATPase (ATP synthase complex) is part of the stalk connecting the F1 and F0 moieties. Studies in Escherichia coli suggest that the analogous bacterial subunit, called epsilon, is essential for the ATPase assembly energy coupling. Platelet-derived growth factor (PDGF) is an important growth factor for various cell types, including neurons of the CNS. Using two-dimensional gel electrophoresis, microsequencing, western blot analysis, and immunoprecipitation techniques, we have found that PDGF induces phosphorylation of the delta subunit or a closely related peptide in cultured mouse cortical neurons.
Zhang
F X
FX
Department of Anatomy, University of Mississippi Medical Center, Jackson 39216, USA.
Pan
W
W
Hutchins
J B
JB
D000818:Animals; D015153:Blotting, Western; D002478:Cells, Cultured; D002540:Cerebral Cortex / Q000166:cytology / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D051379:Mice; D008810:Mice, Inbred C57BL; D025261:Mitochondrial Proton-Translocating ATPases; D009474:Neurons / Q000378:metabolism*; D010766:Phosphorylation; D010982:Platelet-Derived Growth Factor / Q000502:physiology*; D011233:Precipitin Tests; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D010982:Platelet-Derived Growth Factor; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases; C000602561:Atp5d protein, mouse