FH5,RMD,BUI1

2015-01-20 | Categories genes  | Tags chloroplast  panicle  growth  seed  dwarf  seedling  inflorescence  cell elongation  pollen  grain  gravitropic response  root  crown  crown root  phosphate  shoot gravitropism  shoot  auxin 

• Information
  • Symbol: FH5,RMD,BUI1
  • MSU: LOC_Os07g40510,LOC_Os07g40520
  • RAPdb: Os07g0596300
• Publication
  • BENT UPPERMOST INTERNODE1 encodes the class II formin FH5 crucial for actin organization and rice development, 2011, Plant Cell.
  • RICE MORPHOLOGY DETERMINANT encodes the type II formin FH5 and regulates rice morphogenesis, 2011, Plant Cell.
  • Rice actin-binding protein RMD is a key link in the auxin-actin regulatory loop that controls cell growth, 2014, Proceedings of the National Academy of Sciences.
  • Rice Morphology Determinant-mediated Actin Filament Organization Contributes to Pollen Tube Growth., 2018, Plant Physiol.
  • Rice actin binding protein RMD controls crown root angle in response to external phosphate., 2018, Nat Commun.
  • The rice actin-binding protein RMD regulates light-dependent shoot gravitropism., 2019, Plant Physiol.
• Genbank accession number
  • HQ123580
  • AK120222
  • HQ123580
  • AK120222
• Key message
  • FH5/RMD is ubiquitously expressed in rice tissues, and its protein localization to the chloroplast surface is mediated by the PTEN domain
  • The rmd mutants display a bending growth pattern in seedlings, are stunted as adult plants, and have aberrant inflorescence (panicle) and seed shape
  • Cytological observation indicated that the growth defects of bui1 were caused mainly by inhibition of cell expansion
  • The bui1 mutant displayed pleiotropic phenotypes, including bent uppermost internode, dwarfism, wavy panicle rachis, and enhanced gravitropic response
  • Cytological analysis showed that rmd mutants have severe cell elongation defects and abnormal microtubule and microfilament arrays
  • The rice rmd mutant exhibits abnormal pollen tube growth and a decreased germination rate of the pollen grain in vitro and in vivo
  • The rmd pollen tubes display a disorganized F-actin pattern with disrupted apical actin density and shank longitudinal cable direction/arrangement, indicating the novel role of RMD in F-actin polarity during tip growth
  • Consistent with this role, RMD localizes at the tip of the rice pollen tube, which is essential for pollen tube growth and polarity as well as F-actin organization
  • Collectively, our results suggest that RMD is essential for the spatial regulation in pollen tube growth via modulating F-actin organization and array orientation in rice
  • RMD protein localizes to the surface of statoliths, and rmd mutants exhibit faster gravitropic response owing to more rapid statoliths movement
  • Rice actin binding protein RMD controls crown root angle in response to external phosphate.
  • RMD is upregulated in response to low external phosphate and mutants lacking of RMD have steeper crown root growth angles that are unresponsive to phosphate levels
  • We conclude that adaptive changes to root angle in response to external phosphate availability are RMD dependent, providing a potential target for breeders
  • The rice actin-binding protein RMD regulates light-dependent shoot gravitropism.
  • By contrast, etiolated rmd shoots displayed normal negative shoot gravitropism
  • Furthermore, we show that RMD maintains an actin configuration that promotes statolith mobility in gravisensing endodermal cells, and for proper auxin distribution in light-grown, but not dark-grown, shoots
• Connection
  • FH5~RMD~BUI1, OsARF24, Rice actin-binding protein RMD is a key link in the auxin-actin regulatory loop that controls cell growth, Moreover, RMD expression is directly regulated by heterodimerized O. sativa auxin response factor 23 (OsARF23) and OsARF24, providing evidence that auxin modulates the orientation of F-actin arrays through RMD.
  • FH5~RMD~BUI1, OsARF24, Rice actin-binding protein RMD is a key link in the auxin-actin regulatory loop that controls cell growth, In support of this regulatory loop, osarf23 and lines with reduced expression of both OsARF23 and OsARF24 display reduced RMD expression, disrupted F-actin organization and cell growth, less sensitivity to auxin response, and altered auxin distribution and OsPIN localization.
  • APG~OsPIL16, FH5~RMD~BUI1, The rice actin-binding protein RMD regulates light-dependent shoot gravitropism., RMD gene expression is diurnally controlled and directly repressed by the phytochrome-interacting factor-like protein OsPIL16
  • APG~OsPIL16, FH5~RMD~BUI1, The rice actin-binding protein RMD regulates light-dependent shoot gravitropism., Consequently, over-expression of OsPIL16 led to gravisensing and actin patterning defects that phenocopied the rmd mutant
  • FH5~RMD~BUI1, OsERF34, ETHYLENE RESPONSE FACTOR 34 promotes secondary cell wall thickening and strength of rice peduncles., OsERF34 and RMD are highly expressed in sclerenchymatous peduncle cells that are fortified by thick secondary cell walls (SCWs) that provide mechanical peduncle strength

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