Supplementary Materials

Supplementary Materials for:

Binding of the sphingolipid S1P to hTERT stabilizes telomerase at the nuclear periphery by allosterically mimicking protein phosphorylation

Shanmugam Panneer Selvam, Ryan M. De Palma, Joshua J. Oaks, Natalia Oleinik, Yuri K. Peterson, Robert V. Stahelin, Emmanuel Skordalakes, Suriyan Ponnusamy, Elizabeth Garrett-Mayer, Charles D. Smith, Besim Ogretmen*

*Corresponding author. E-mail: ogretmen{at}musc.edu

This PDF file includes:

  • Fig. S1. Roles of SK1 versus SK2 on hTERT abundance and 17C-S1P binding.
  • Fig. S2. S1P-TERT binding is mediated by the C′3-OH of S1P and the hydrophobic region of TERT between the thumb and finger domains.
  • Fig. S3. hTERT colocalizes with lamin B at the nuclear periphery.
  • Fig. S4. Detection of stably expressed hTERT in MEFs.
  • Fig. S5. Effects of S1P-hTERT binding on hTERT-MKRN1 interaction and growth inhibition in response to GA treatment.
  • Fig. S6. S1P binding might mimic protein phosphorylation of hTERT at Ser921.
  • Fig. S7. Effects of SK2-generated S1P on hTERT-dependent senescence.
  • Fig. S8. Regulation of senescence by S1P-hTERT binding in wild-type or SK2-deficient MEFs.

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Citation: S. Panneer Selvam, R. M. De Palma, J. J. Oaks, N. Oleinik, Y. K. Peterson, R. V. Stahelin, E. Skordalakes, S. Ponnusamy, E. Garrett-Mayer, C. D. Smith, B. Ogretmen, Binding of the sphingolipid S1P to hTERT stabilizes telomerase at the nuclear periphery by allosterically mimicking protein phosphorylation. Sci. Signal. 8, ra58 (2015).

© 2015 American Association for the Advancement of Science