Disease relevance of PTC2

• Deleting PTC2 specifically suppresses the hydroxyurea hypersensitivity of mec1 mutants and the lethality of mec1Delta [1].

High impact information on PTC2

• In contrast, overexpression of PTC2 rescues adaptation-defective yku80Delta and cdc5-ad mutants [2].
• PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break [2].
• Cells lacking the PP2C-like phosphatases Ptc2 and Ptc3 are unable to adapt to a HO-induced DSB and are also defective in recovering from a repairable DSB [2].
• These results demonstrate that Ptc2p downregulates the UPR by dephosphorylating Ire1p and reveal a novel mechanism of regulation in the UPR pathway upstream of the HAC1 mRNA splicing event [3].
• Searching for proteins that interact with Ire1p in Saccharomyces cerevisiae, we isolated PTC2, which encodes a serine/threonine phosphatase of type 2C [3].

Biological context of PTC2

• Thus Ptc2 requires an additional amino acid sequence beyond the catalytic domain defined for PTCs for full activity [4].
• The Ptc2p interaction with Ire1p is specific, direct, dependent on Ire1p phosphorylation, and mediated through a kinase interaction domain within Ptc2p [3].

Associations of PTC2 with chemical compounds

• Role of Ptc2 type 2C Ser/Thr phosphatase in yeast high-osmolarity glycerol pathway inactivation [4].
• Protein serine/threonine phosphatase Ptc2p negatively regulates the unfolded-protein response by dephosphorylating Ire1p kinase [3].
• Ret/ptc2 is a constitutively active, oncogenic form of the c-Ret receptor tyrosine kinase [5].

Other interactions of PTC2

• Three type 2C Ser/Thr phosphatases (PTCs), Ptc1, Ptc2, and Ptc3, have been isolated as negative regulators of this pathway [6].
• Strains carrying null alleles of PTC2 have a three- to fourfold-increased UPR and increased levels of spliced HAC1 mRNA [3].
• The ire1 and ptc2 genes involved in the unfolded protein response pathway in the filamentous fungus Trichoderma reesei [7].

References