TY - JOUR
T1 - Trifluoperazine and W-7 inhibit mating in Chlamydomonas at an early stage of gametic interaction
AU - Detmers, Patricia A.
AU - Condeelis, John
N1 - Funding Information:
We would like to thank Dr T. Otter for usefuld iscussionsd uringthe courseo f the work and Dr S. D. Wright for helpful suggestionso n the manuscript. The work was supported by a research fellowship from the New York Heart Associationt o P. D., an institutionagl rantt o AECOM from the American Cancer Society and GM25813,a nd a Hirsch1C areer Scientist Award to J. C. P. D. is an Arthritis Foundation investigator.
PY - 1986/4
Y1 - 1986/4
N2 - Gametic mating by Chlamydomonas reinhardi is inhibited in a dose-dependent and reversible manner by the calmodulin antagonists trifluoperazine (TFP) and W-7, but not by W-5, an analog of W-7 having lower affinity for calmodulin. Quantitation of the sequential steps of mating showed that TFP and W-7 both allow normal levels of flagellar agglutination but prevent all subsequent steps. Gametes agglutinate aberrantly and do not form mating pairs. Further, both of these drugs prevent the translocation of latex beads along the flagellar surface. Our observations suggest that calmodulin may play an integral role in the translocation of flagellar adhesion sites during the tip-locking stage of the Chlamydomonas mating reaction. Flagellar surface motility may be crucial to the transduction of signals during mating and may share regulatory mechanisms with other forms of surface motility.
AB - Gametic mating by Chlamydomonas reinhardi is inhibited in a dose-dependent and reversible manner by the calmodulin antagonists trifluoperazine (TFP) and W-7, but not by W-5, an analog of W-7 having lower affinity for calmodulin. Quantitation of the sequential steps of mating showed that TFP and W-7 both allow normal levels of flagellar agglutination but prevent all subsequent steps. Gametes agglutinate aberrantly and do not form mating pairs. Further, both of these drugs prevent the translocation of latex beads along the flagellar surface. Our observations suggest that calmodulin may play an integral role in the translocation of flagellar adhesion sites during the tip-locking stage of the Chlamydomonas mating reaction. Flagellar surface motility may be crucial to the transduction of signals during mating and may share regulatory mechanisms with other forms of surface motility.
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U2 - 10.1016/0014-4827(86)90063-7
DO - 10.1016/0014-4827(86)90063-7
M3 - Article
C2 - 3956581
AN - SCOPUS:0022454119
VL - 163
SP - 317
EP - 326
JO - Experimental Cell Research
JF - Experimental Cell Research
SN - 0014-4827
IS - 2
ER -