Pennsylvania State University
ORCID: 0000-0002-8004-4817Publishes on Autophagy in Disease and Therapy, Physics of Superconductivity and Magnetism, Magnetic and transport properties of perovskites and related materials. 220 papers and 18.2k citations.
Add your photo, update your bio, and get notified when your ranking changes.
Spin fluctuations in antiferromagnetic and nearly antiferromagnetic two dimensional (square lattice) itinerant electron systems, as a possible model for high T c superconductors, are investigated by using the self-consistent renormalization theory. The electrical resistivity and the nuclear spin relaxation rate due to the spin fluctuations in the normal state are calculated. The results in the nearly antiferromagnetic regime as applied to high T c oxides seem to explain the experimental results both in their temperature dependence and in their orders of magnitudes. By using the same spin fluctuations we discuss superconductivity due to the spin fluctuation mechanism within a weak coupling theory. The order parameter is shown to have B 1 g or A 2 g symmetry and the critical temperature is evaluated to be of the right order of magnitude.
Autophagy is a highly orchestrated intracellular bulk degradation process that is activated by various environmental stresses. The serine/threonine kinase ULK1, like its yeast homologue Atg1, is a key initiator of autophagy that is negatively regulated by the mTOR kinase. However, the molecular mechanism that controls the inhibitory effect of mTOR on ULK1-mediated autophagy is not fully understood. Here we identified AMPK, a central energy sensor, as a new ULK1-binding partner. We found that AMPK binds to the PS domain of ULK1 and this interaction is required for ULK1-mediated autophagy. Interestingly, activation of AMPK by AICAR induces 14-3-3 binding to the AMPK-ULK1-mTORC1 complex, which coincides with raptor Ser792 phosphorylation and mTOR inactivation. Consistently, AICAR induces autophagy in TSC2-deficient cells expressing wild-type raptor but not the mutant raptor that lacks the AMPK phosphorylation sites (Ser722 and Ser792). Taken together, these results suggest that AMPK association with ULK1 plays an important role in autophagy induction, at least in part, by phosphorylation of raptor to lift the inhibitory effect of mTOR on the ULK1 autophagic complex.