The study highlights the interaction between Hsp90-Cdc37 and ULK1.


The study highlights the interaction between Hsp90-Cdc37 and ULK1, a kinase that the authors show, the removal and the removal and disposal of damaged mitochondria. Cdc37 and Hsp90 stabilized activated ULK1, which in turn phosphorylates its substrate Atg13 released from the complex released from the complex. Atg13 then eliminate damaged mitochondria through autophagy. Thus, the study links Hsp90-Cdc37 ULK1 – Atg13 in a direct way, the essential condition for efficient mitochondrial clearance. ‘The new study shows that the key regulatory mechanism of this process , the Hsp90 chaperone Cdc37, as the on-off switch, does that crucial for the correct function of ULK1 kinase, ‘Cleveland said.

You can view the entire Kaiser Daily Global Health Policy Report search the archives and sign up for email delivery of global health.. Hsp90 is a heat shock protein, a cell of the most abundant proteins and helps in everything from protein folding and tumor cell signaling repression. Also a protein, is a co-chaperone Hsp90 on and is in cell signal transduction and connecting kinases kinases may add a phosphate group to various molecules and modify protein activity ) on the right kinases involved.

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