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Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (limited proteolysis experiment)

ABSTRACT: The charged linker region in Hsp90 has been shown to be important for Hsp90 function and global conformation. In humans, two serines located in the charged linker region are constitutively phosphorylated in vivo. In order to gain knowledge on the possible effect of these phosphorylation sites on Hsp90 global conformation, we purified a human Hsp90β mutant where both serines are mutated to alanines, and used limited proteolysis to study the “proteolytic” fingerprint of our mutant and the wild-type, phosphorylated Hsp90β. We observed that serine to alanine mutation resulted in increased tryptic cleavage in the C-domain of Hsp90β.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Manfredo Quadroni

LAB HEAD: Manfredo Quadroni

PROVIDER: PXD025878 | Pride | 2021-07-07

REPOSITORIES: Pride

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			Action	DRS
	210203_LW_12853-LiP2-0ng-A.mzid.gz	Mzid
	210203_LW_12853-LiP2-0ng-A.raw	Raw
	210203_LW_12853-LiP2-0ng-B.mzid.gz	Mzid
	210203_LW_12853-LiP2-0ng-B.raw	Raw
	210203_LW_12853-LiP2-0ng-C.mzid.gz	Mzid

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Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (limited proteolysis experiment)

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