Gravisensing: ionic responses, cytoskeleton and amyloplast behavior.
In Zea mays L., changes in orientation of stems are perceived by the pulvinal tissue, which responds to the stimulus by differential growth resulting in upward bending of the stem. Gravity is perceived in the bundle sheath cells, which contain amyloplasts that sediment to the new cell base when a change in the gravity vector occurs. The mechanism by which the mechanical signal is transduced into a physiological response is so far unknown for any gravity perceiving tissue. It is hypothesized that this involves interactions of amyloplasts with the plasma membrane and/or ER via cytoskeletal elements. To gain further insights into this process we monitored amyloplast movements in response to gravistimulation. In a pharmacological approach we investigated how the dynamics of plastid sedimentation are affected by actin and microtubule (MT) disrupting drugs. Dark grown caulonemal filaments of the moss Physcomitrella patens respond to gravity vector changes with a reorientation of tip growth away from the gravity vector. MT distributions in tip cells were monitored over time and MTs were seen to accumulate preferentially on the lower flank of the tip 30 min after a 90 degree turn. Using a self-referencing Ca2+ selective ion probe, we found that growing caulonemal filaments exhibit a Ca2+ influx at the apical dome, similar to that reported previously for other tip growing cells. However, in gravistimulated Physcomitrella filaments the region of Ca2+ influx is not confined to the apex, but extends about 60 micrometers along the upper side of the filament. Our results indicate an asymmetry in the Ca2+ flux pattern between the upper and side of the filament suggesting differential activation of Ca2+ permeable channels at the plasma membrane.
Allen
N Strömgren
NS
Department of Botany, North Carolina State University, Raleigh, NC 27695-7612, USA. nina_allen@ncsu.edu
Chattaraj
P
P
Collings
D
D
Johannes
E
E
D008841:Actin Cytoskeleton / Q000502:physiology; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D019068:Bryopsida / Q000502:physiology / Q000648:ultrastructure; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000378:metabolism; D003599:Cytoskeleton / Q000502:physiology; D003624:Darkness; D004136:Dinitrobenzenes / Q000494:pharmacology; D018522:Gravitropism / Q000502:physiology*; D018466:Gravity Sensing / Q000502:physiology*; D006540:Herbicides / Q000494:pharmacology; D008387:Marine Toxins / Q000494:pharmacology; D018613:Microscopy, Confocal; D008870:Microtubules / Q000502:physiology*; D018520:Plant Shoots / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D018087:Plastids / Q000187:drug effects / Q000502:physiology*; D018516:Pulvinus / Q000187:drug effects / Q000502:physiology*; D013424:Sulfanilamides / Q000494:pharmacology; D053778:Thiazolidines / Q000494:pharmacology; D050257:Tubulin Modulators / Q000494:pharmacology; D003313:Zea mays / Q000502:physiology / Q000648:ultrastructure
D019086:Bridged Bicyclo Compounds, Heterocyclic; D015220:Calcium Channels; D004136:Dinitrobenzenes; D006540:Herbicides; D008387:Marine Toxins; D013424:Sulfanilamides; D053778:Thiazolidines; D050257:Tubulin Modulators; C012465:oryzalin; C037068:latrunculin B; D002118:Calcium