User:Iris To/Retinoblastoma Protein Regulation: Difference between revisions
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It has been found that PP1c directly inhibits phosphorylation of RbC from Cdk2-CycA[http://www.neb.com/nebecomm/products/productp6025.asp]; it is not affected by phosphatase activity but by the presence of the KLRF docking site, which binds the catalytic subunit of PP1c to a specific site of Rb<ref name=Hirschi>PMID: 20694007</ref>. In addition, it has been observed that PP1c makes complexes with RbC when there are many phosphatases produced, thus overthrowing Cdk activity and inhibiting cell progression from the G1 phase. This competition is important in terms of cell signaling, which is affected by response to cellular stress, cell cycle exit, DNA damage, etc<ref name=Hirschi>PMID: 20694007</ref>. This is because the competition further controls cell overgrowth besides phosphorylation regulation. Studies determined a biochemical mechanism where directly competing kinases and phosphatase activity regulates Rb phosphorylation and activity, but there has not been an established study that defined a mechanism that controlled the outcome of the competition between each enzyme<ref name=Hirschi>PMID: 20694007</ref>. | It has been found that PP1c directly inhibits phosphorylation of RbC from Cdk2-CycA[http://www.neb.com/nebecomm/products/productp6025.asp]; it is not affected by phosphatase activity but by the presence of the KLRF docking site, which binds the catalytic subunit of PP1c to a specific site of Rb<ref name=Hirschi>PMID: 20694007</ref>. In addition, it has been observed that PP1c makes complexes with RbC when there are many phosphatases produced, thus overthrowing Cdk activity and inhibiting cell progression from the G1 phase. This competition is important in terms of cell signaling, which is affected by response to cellular stress, cell cycle exit, DNA damage, etc<ref name=Hirschi>PMID: 20694007</ref>. This is because the competition further controls cell overgrowth besides phosphorylation regulation. Studies determined a biochemical mechanism where directly competing kinases and phosphatase activity regulates Rb phosphorylation and activity, but there has not been an established study that defined a mechanism that controlled the outcome of the competition between each enzyme<ref name=Hirschi>PMID: 20694007</ref>. | ||
<StructureSection load='3n5u' size='500' side='right' caption='Structure of Rb-PP1c(PDB entry [[3n5u]])' scene=''> | |||
==Structure and Function== | ==Structure and Function== | ||
PP1[http://www.signaling-gateway.org/update/images/su-0406-3-i1.jpg] | PP1[http://www.signaling-gateway.org/update/images/su-0406-3-i1.jpg] | ||
<scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/2'>Rb binds PP1c with an extended conformation at hydrophobic interface</scene> | <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/2'>Rb binds PP1c with an extended conformation at hydrophobic interface</scene> | ||
