ULK2 is a serine/threonine protein kinase that plays critical role during initial stages of autophagy which is a vital response to nutrient starvation. Mammalian Atg13 binds ULK2 and mediates the interaction of the ULK protein with FIP200. The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK. The ULK-Atg13-FIP200 complex is a direct target of mTOR and important regulator of autophagy in response to mTOR signalling. Yeast 2-hybrid assays showed the C-terminus of ULK2 binds the C-terminus of SynGAP, a negative regulator of Ras that is associated with neural development.
Previous studies showed that the serine/threonine kinase Unc51.1 is one of the earliest genes in neuronal differentiation and is required for granule cell axon formation. To examine the mechanism of Unc51.1 regulation of axon extension, we have identified two direct
Molecular biology of the cell, 20(7), 1992-2003 (2009-02-20)
Autophagy, the starvation-induced degradation of bulky cytosolic components, is up-regulated in mammalian cells when nutrient supplies are limited. Although mammalian target of rapamycin (mTOR) is known as the key regulator of autophagy induction, the mechanism by which mTOR regulates autophagy
The biogenesis of small uridine-rich nuclear ribonucleoproteins (UsnRNPs) depends on the methylation of Sm proteins catalyzed by the methylosome and the subsequent action of the SMN complex, which assembles the heptameric Sm protein ring onto small nuclear RNAs (snRNAs). In
Disturbances in autophagy and stress granule dynamics have been implicated as potential mechanisms underlying inclusion body myopathy (IBM) and related disorders. Yet the roles of core autophagy proteins in IBM and stress granule dynamics remain poorly characterized. Here, we demonstrate
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