Score: 7.00 | Title: An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity .
| Author: Chen X Chern M Canlas PE Ruan D Jiang C Ronald PC | Journal: Proc Natl Acad Sci U S A Citation: V : 107 P : 8029-34 Year: 2010 | Literature: oryza Field: abstract Doc ID: pub20385831 Accession (PMID): 20385831 | Abstract: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants .
These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling .
Despite their importance , the mode of regulation of PRRs is largely unknown .
Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase .
XB24 promotes autophosphorylation of XA21 through its ATPase activity .
Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity .
XB24 ATPase enzyme activity is required for XB24 function .
XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed .
These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity .
| Matching Sentences: [ Sen. 6, subscore: 2.00 ]: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants . These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling . Despite their importance , the mode of regulation of PRRs is largely unknown . Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase . XB24 promotes autophosphorylation of XA21 through its ATPase activity . Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity . XB24 ATPase enzyme activity is required for XB24 function . XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed . These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity . [ Sen. 7, subscore: 2.00 ]: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants . These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling . Despite their importance , the mode of regulation of PRRs is largely unknown . Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase . XB24 promotes autophosphorylation of XA21 through its ATPase activity . Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity . XB24 ATPase enzyme activity is required for XB24 function . XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed . These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity . [ Sen. 4, subscore: 1.00 ]: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants . These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling . Despite their importance , the mode of regulation of PRRs is largely unknown . Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase . XB24 promotes autophosphorylation of XA21 through its ATPase activity . Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity . XB24 ATPase enzyme activity is required for XB24 function . XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed . These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity . [ Sen. 5, subscore: 1.00 ]: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants . These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling . Despite their importance , the mode of regulation of PRRs is largely unknown . Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase . XB24 promotes autophosphorylation of XA21 through its ATPase activity . Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity . XB24 ATPase enzyme activity is required for XB24 function . XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed . These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity . [ Sen. 8, subscore: 1.00 ]: Cell-surface pattern recognition receptors ( PRRs ) are key components of the innate immune response in animals and plants . These receptors typically carry or associate with non-RD kinases to control early events of innate immunity signaling . Despite their importance , the mode of regulation of PRRs is largely unknown . Here we show that the rice PRR , XA21 , interacts with XA21 binding protein 24 ( XB24 ) , a previously undescribed ATPase . XB24 promotes autophosphorylation of XA21 through its ATPase activity . Rice lines silenced for Xb24 display enhanced XA21-mediated immunity , whereas rice lines overexpressing XB24 are compromised for immunity . XB24 ATPase enzyme activity is required for XB24 function . XA21 is degraded in the presence of the pathogen-associated molecular pattern Ax21 when XB24 is overexpressed . These results demonstrate a function for this large class of broadly conserved ATPases in PRR-mediated immunity .
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