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| Title: The rice dynamin-related protein DRP2B mediates membrane trafficking , and thereby plays a critical role in secondary cell wall cellulose biosynthesis .
| | Author: Xiong G Li R Qian Q Song X Liu X Yu Y Zeng D Wan J Li J Zhou Y | | Journal: Plant J Citation: V : 64 P : 56-70 Year: 2010 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub20663087 Accession (PMID): 20663087 | | Abstract: Membrane trafficking between the plasma membrane ( PM ) and intracellular compartments is an important process that regulates the deposition and metabolism of cell wall polysaccharides .
Dynamin-related proteins ( DRPs ) , which function in membrane tubulation and vesiculation are closely associated with cell wall biogenesis .
However , the molecular mechanisms by which DRPs participate in cell wall formation are poorly understood .
Here , we report the functional characterization of Brittle Culm3 ( BC3 ) , a gene encoding OsDRP2B .
Consistent with the expression of BC3 in mechanical it issues , the bc3 mutation reduces mechanical strength , which results from decreased cellulose content and altered secondary wall structure .
OsDRP2B , one of three members of the DRP2 subfamily in rice ( Oryza sativa L ) , was identified as an authentic membrane-associated dynamin via in vitro biochemical analyses .
Subcellular localization of fluorescence-tagged OsDRP2B and several compartment markers in protoplast cells showed that this protein not only lies at the PM and the clathrin-mediated vesicles , but also is targeted to the trans-Golgi network ( TGN ) .
An FM4-64 uptake assay in transgenic plants that express green fluorescent protein-tagged OsDRP2B verified its involvement in an endocytic pathway .
BC3 mutation and overexpression altered the abundance of cellulose synthase catalytic subunit 4 ( OsCESA4 ) in the PM and in the endomembrane systems .
All of these findings lead us to conclude that OsDRP2B participates in the endocytic pathway , probably as well as in post-Golgi membrane trafficking .
Mutation of OsDRP2B disturbs the membrane trafficking that is essential for normal cellulose biosynthesis of the secondary cell wall , thereby leading to inferior mechanical properties in rice plants .
| Matching Sentences:
[ Sen. 6, subscore: 1.00 ]: Dynamin-related proteins ( DRPs ) , which function in membrane tubulation and vesiculation are closely associated with cell wall biogenesis . However , the molecular mechanisms by which DRPs participate in cell wall formation are poorly understood . Here , we report the functional characterization of Brittle Culm3 ( BC3 ) , a gene encoding OsDRP2B . Consistent with the expression of BC3 in mechanical it issues , the bc3 mutation reduces mechanical strength , which results from decreased cellulose content and altered secondary wall structure . OsDRP2B , one of three members of the DRP2 subfamily in rice ( Oryza sativa L ) , was identified as an authentic membrane-associated dynamin via in vitro biochemical analyses . Subcellular localization of fluorescence-tagged OsDRP2B and several compartment markers in protoplast cells showed that this protein not only lies at the PM and the clathrin-mediated vesicles , but also is targeted to the trans-Golgi network ( TGN ) . An FM4-64 uptake assay in transgenic plants that express green fluorescent protein-tagged OsDRP2B verified its involvement in an endocytic pathway . BC3 mutation and overexpression altered the abundance of cellulose synthase catalytic subunit 4 ( OsCESA4 ) in the PM and in the endomembrane systems . All of these findings lead us to conclude that OsDRP2B participates in the endocytic pathway , probably as well as in post-Golgi membrane trafficking .
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Score: 1.00 |
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| Title: The rice dynamin-related protein DRP2B mediates membrane trafficking , and thereby plays a critical role in secondary cell wall cellulose biosynthesis .
| | Author: Xiong G Li R Qian Q Song X Liu X Yu Y Zeng D Wan J Li J Zhou Y | | Journal: Plant J Citation: V : 64 P : 56-70 Year: 2010 Type: MEDLINE | | Literature: oryza Field: title Doc ID: pub20663087 Accession (PMID): 20663087 | | Abstract: Membrane trafficking between the plasma membrane ( PM ) and intracellular compartments is an important process that regulates the deposition and metabolism of cell wall polysaccharides .
Dynamin-related proteins ( DRPs ) , which function in membrane tubulation and vesiculation are closely associated with cell wall biogenesis .
However , the molecular mechanisms by which DRPs participate in cell wall formation are poorly understood .
Here , we report the functional characterization of Brittle Culm3 ( BC3 ) , a gene encoding OsDRP2B .
Consistent with the expression of BC3 in mechanical it issues , the bc3 mutation reduces mechanical strength , which results from decreased cellulose content and altered secondary wall structure .
OsDRP2B , one of three members of the DRP2 subfamily in rice ( Oryza sativa L ) , was identified as an authentic membrane-associated dynamin via in vitro biochemical analyses .
Subcellular localization of fluorescence-tagged OsDRP2B and several compartment markers in protoplast cells showed that this protein not only lies at the PM and the clathrin-mediated vesicles , but also is targeted to the trans-Golgi network ( TGN ) .
An FM4-64 uptake assay in transgenic plants that express green fluorescent protein-tagged OsDRP2B verified its involvement in an endocytic pathway .
BC3 mutation and overexpression altered the abundance of cellulose synthase catalytic subunit 4 ( OsCESA4 ) in the PM and in the endomembrane systems .
All of these findings lead us to conclude that OsDRP2B participates in the endocytic pathway , probably as well as in post-Golgi membrane trafficking .
Mutation of OsDRP2B disturbs the membrane trafficking that is essential for normal cellulose biosynthesis of the secondary cell wall , thereby leading to inferior mechanical properties in rice plants .
| Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: The rice dynamin-related protein DRP2B mediates membrane trafficking , and thereby plays a critical role in secondary cell wall cellulose biosynthesis .
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