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| 2. |
- Puustinen, J., et al.
(författare)
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1.22 µm GaInNAs saturable absorber mirrors with tailored recovery time
- 2010
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Ingår i: Emerging trends and novel materials in photonics. - : American Institute of Physics (AIP). - 9780735408432 ; , s. 200-203
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Konferensbidrag (refereegranskat)abstract
- The effect of in-situ N-ion irradiation on the recombination dynamics of GaInNAs/GaAs semiconductor saturable absorber mirrors has been studied. The samples were fabricated by molecular beam epitaxy using a radio frequency plasma source for nitrogen incorporation in the absorber layers as well as for the irradiation. The recombination dynamics of irradiated samples were studied by pump-probe measurements. The recombination time of the absorbers could be reduced by increasing the irradiation time. The effect of the reduced recombination time on the pulse dynamics of a mode-locked laser setup was studied with a Bi-doped fibre laser. The pulse quality was found to improve with increased irradiation time and reduced recombination time, demonstrating the potential of the in-situ irradiation method for device applications.
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| 3. |
- Puustinen, P, et al.
(författare)
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CIP2A oncoprotein controls cell growth and autophagy through mTORC1 activation
- 2014
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Ingår i: The Journal of cell biology. - : Rockefeller University Press. - 1540-8140 .- 0021-9525. ; 204:5, s. 713-727
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Tidskriftsartikel (refereegranskat)abstract
- mTORC1 (mammalian target of rapamycin complex 1) integrates information regarding availability of nutrients and energy to coordinate protein synthesis and autophagy. Using ribonucleic acid interference screens for autophagy-regulating phosphatases in human breast cancer cells, we identify CIP2A (cancerous inhibitor of PP2A [protein phosphatase 2A]) as a key modulator of mTORC1 and autophagy. CIP2A associates with mTORC1 and acts as an allosteric inhibitor of mTORC1-associated PP2A, thereby enhancing mTORC1-dependent growth signaling and inhibiting autophagy. This regulatory circuit is reversed by ubiquitination and p62/SQSTM1-dependent autophagic degradation of CIP2A and subsequent inhibition of mTORC1 activity. Consistent with CIP2A’s reported ability to protect c-Myc against proteasome-mediated degradation, autophagic degradation of CIP2A upon mTORC1 inhibition leads to destabilization of c-Myc. These data characterize CIP2A as a distinct regulator of mTORC1 and reveals mTORC1-dependent control of CIP2A degradation as a mechanism that links mTORC1 activity with c-Myc stability to coordinate cellular metabolism, growth, and proliferation.
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