Supplementary Materials

Supplementary Materials for:

PIP4kγ is a substrate for mTORC1 that maintains basal mTORC1 signaling during starvation

Ashley M. Mackey, Deborah A. Sarkes, Ian Bettencourt, John M. Asara, Lucia E. Rameh*

*Corresponding author. E-mail: rameh{at}bu.edu

This PDF file includes:

  • Fig. S1. PIP4kγ knockdown decreases cell size and mTORC1 signaling in serum- or amino acid–starved Tsc2 knockdown cells and identification of mTORC1-dependent phosphorylation sites in PIP4kγ.
  • Fig. S2. Phosphorylation of PIP4kγ does not affect protein stability, dimerization, or associated kinase activity or cellular PI-5-P.
  • Fig. S3. PIP4kγ localizes to cytosolic and Golgi-associated vesicles.
  • Fig. S4. Analysis of the effect of rapamycin on the distribution of PIP4kγ, GM130, or βCOP among the four fractions generated by differential centrifugation of BTC6 cells.

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Citation: A. M. Mackey, D. A. Sarkes, I. Bettencourt, J. M. Asara, L. E. Rameh, PIP4kγ is a substrate for mTORC1 that maintains basal mTORC1 signaling during starvation. Sci. Signal. 7, ra104 (2014).

© 2014 American Association for the Advancement of Science