TY - JOUR
T1 - Actin-microtubule interactions in the alga Nitella
T2 - Analysis of the mechanism by which microtubule depolymerization potentiates cytochalasin's effects on streaming
AU - Collings, DA
AU - Wasteneys, GO
AU - Williamson, RE
PY - 1996
Y1 - 1996
N2 - In the characean alga Nitella, depolymerization of microtubules potentiates the inhibitory effects of cytochalasins on cytoplasmic streaming. Microtubule depolymerization lowers the cytochalasin B and D concentrations required to inhibit streaming, accelerates inhibition and delays streaming recovery. Because microtubule depolymerization does nor significantly alter H-3-cytochalasin B uptake and release, elevated intracellular cytochalasin concentrations are not the basis for potentiation. Instead, microtubule depolymerization causes actin to become more sensitive to cytochalasin. This increased sensitivity of actin is unlikely to be due to direct stabilization of actin by microtubules, however, because very few microtubules colocalize with the subcortical actin bundles that generate streaming. Furthermore, microtubule reassembly, but nor recovery of former transverse alignment, is sufficient for restoring the normal cellular responses to cytochalasin D. We hypothesize that either tubulin or microtubule-associated proteins, released when microtubules depolymerize, interact with the actin cytoskeleton and sensitize it to cytochalasin.
AB - In the characean alga Nitella, depolymerization of microtubules potentiates the inhibitory effects of cytochalasins on cytoplasmic streaming. Microtubule depolymerization lowers the cytochalasin B and D concentrations required to inhibit streaming, accelerates inhibition and delays streaming recovery. Because microtubule depolymerization does nor significantly alter H-3-cytochalasin B uptake and release, elevated intracellular cytochalasin concentrations are not the basis for potentiation. Instead, microtubule depolymerization causes actin to become more sensitive to cytochalasin. This increased sensitivity of actin is unlikely to be due to direct stabilization of actin by microtubules, however, because very few microtubules colocalize with the subcortical actin bundles that generate streaming. Furthermore, microtubule reassembly, but nor recovery of former transverse alignment, is sufficient for restoring the normal cellular responses to cytochalasin D. We hypothesize that either tubulin or microtubule-associated proteins, released when microtubules depolymerize, interact with the actin cytoskeleton and sensitize it to cytochalasin.
KW - Nitella
KW - Actin
KW - Cytochalasin
KW - Cytoplasmic streaming
KW - Microtubule depolymerization
KW - Oryzalin
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=anu_research_portal_plus2&SrcAuth=WosAPI&KeyUT=WOS:A1996UK03000008&DestLinkType=FullRecord&DestApp=WOS_CPL
U2 - 10.1007/BF01281816
DO - 10.1007/BF01281816
M3 - Article
SN - 0033-183X
VL - 191
SP - 178
EP - 190
JO - Protoplasma
JF - Protoplasma
IS - 3-4
ER -