Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.82833231 |
Although Pin 1 could interact with Plx 1 during interphase and mitosis , only the phosphorylated , mitotically active form of Cdc 25 was able to bind Pin 1 , an event we have recapitulated using in vitro phosphorylated Cdc 25 . 0.82833231^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Many of these Pin 1 binding proteins are also recognized by the monoclonal antibody MPM 2 , and they include the important mitotic regulators Cdc 25 , Myt 1 , Wee 1 , Plk 1 , and Cdc 27 . ^^^ We have examined the interaction between Pin 1 and Cdc 25 in detail . ^^^ Pin 1 not only binds the mitotic form of Cdc 25 on the phosphorylation sites important for its activity in vitro and in vivo , but it also inhibits its activity , offering one explanation for the ability of Pin 1 to inhibit mitotic entry . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Overexpression of the prolyl isomerase Pin 1 , which binds to the hyperphosphorylated forms of Cdc 25 , Myt 1 , and Wee 1 found at M phase , is known to block the initiation of mitosis in egg extracts . ^^^ We have observed that Pin 1 specifically antagonizes the stimulatory effect of p 9 on phosphorylation of Cdc 25 by Cdc2 / cyclin B . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Premature mitotic entry in the absence of Pin 1 was accompanied by hyperphosphorylation of Cdc 25 , activation of Cdc2 / cyclin B , and generation of epitopes recognized by the mitotic phosphoprotein antibody , MPM 2 . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
No direct interaction between the PIN 1 WW domain or its catalytic proline cis / trans isomerase domain and p 13 ( SUC 1 ) was detected , but our study showed that in vitro the WW domain of the human PIN 1 antagonizes the binding of the p 13 ( SUC 1 ) to the CDC 25 phosphopeptide , by binding to the same phosphoepitope . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
The WW domain of Pin 1 acts as a phosphoserine / threonine binding module binding a defined subset of mitosis specific phosphoproteins , such as Cdc 25 and tau . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Pin 1 acts catalytically to promote a conformational change in Cdc 25 . ^^^ We show that Pin 1 catalytically generates a conformational change on the mitotic phosphatase Cdc 25 , as assayed by limited protease digestion , differential reactivity to a phosphoserine proline directed monoclonal antibody ( MPM 2 ) , and by changes in Cdc 25 enzymatic activity . ^^^ Pin 1 catalytically modifies the conformation of Cdc 25 at stoichiometries less than 0 . 0005 , and mutants of Pin 1 in the prolyl isomerase domain are not active . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Human Pin 1 interacts with mitotic phosphoproteins , such as NIMA , Cdc 25 and Wee 1 , and inhibits G ( 2 ) / M progression in Xenopus extracts . ^^^ Furthermore , the pin 1 Delta allele caused a synthetic growth defect when combined with either cdc 25 22 or wee 1 50 but not the cdc 24 1 temperature sensitive mutant . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Pin 1 interacts with a series of mitotic phosphoproteins , including Polo like kinase 1 , Cdc25C , and Cdc 27 , and is thought to act as a phosphorylation dependent PPIase for these target molecules . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Pin 1 dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins . ^^^ Furthermore , Pin 1 catalyzes prolyl isomerization of specific pSer / Thr Pro motifs both in Cdc25C and tau to facilitate their dephosphorylation by PP2A . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
Pin 1 binds to many proteins implicated in cell cycle regulation ( e . g . p 53 , Myt 1 , Wee 1 , and Cdc25C ) . ^^^ |
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Interacting proteins: P30307 and Q13526 |
Pubmed |
SVM Score :0.0 |
NA |
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