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Plant Physiol, January 2003, Vol. 131, pp. 254-263
Do Phytotropins Inhibit Auxin Efflux by Impairing Vesicle
Traffic?1
Jan
Petrá ek,
Adriana
erná,
Kate ina
Schwarzerová,
Miroslav
El kner,
David
A.
Morris,2 and
Eva
Za ímalová*
Institute of Experimental Botany, The Academy of Sciences of the
Czech Republic, Rozvojová 135, CZ-16502 Prague 6, Czech Republic
(J.P., M.E., D.A.M., E.Z.); and Department of Plant Physiology, Faculty
of Science, Charles University, Vini ná, CZ-12844 Prague
2, Czech Republic (J.P., A. ., K.S.)
Phytotropins such as 1-N-naphthylphthalamic
acid (NPA) strongly inhibit auxin efflux, but the mechanism of this
inhibition remains unknown. Auxin efflux is also strongly decreased by
the vesicle trafficking inhibitor brefeldin A (BFA). Using
suspension-cultured interphase cells of the BY-2 tobacco
(Nicotiana tabacum L. cv Bright-Yellow 2) cell line, we
compared the effects of NPA and BFA on auxin accumulation and on the
arrangement of the cytoskeleton and endoplasmic reticulum (ER). The
inhibition of auxin efflux (stimulation of net accumulation) by both
NPA and BFA occurred rapidly with no measurable lag. NPA had no
observable effect on the arrangement of microtubules, actin filaments,
or ER. Thus, its inhibitory effect on auxin efflux was not mediated by
perturbation of the cytoskeletal system and ER. BFA, however, caused
substantial alterations to the arrangement of actin filaments and ER,
including a characteristic accumulation of actin in the perinuclear
cytoplasm. Even at saturating concentrations, NPA inhibited net auxin
efflux far more effectively than did BFA. Therefore, a proportion of the NPA-sensitive auxin efflux carriers may be protected from the
action of BFA. Maximum inhibition of auxin efflux occurred at
concentrations of NPA substantially below those previously reported to
be necessary to perturb vesicle trafficking. We found no evidence to
support recent suggestions that the action of auxin transport
inhibitors is mediated by a general inhibition of vesicle-mediated protein traffic to the plasma membrane.
1
This work was supported by the European Union,
International Cooperation Copernicus (grant no. ERBIC15 CT98
0118 to E.Z.); by the Ministry of Education, Youth, and Sports of the
Czech Republic (project no. LN00A081); and by the UK Royal Society and
the Academy of Sciences of the Czech Republic under the European
Science Exchange Scheme (grant to D.A.M.).
2
Present address: Division of Cell Sciences, School of
Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK.
*
Corresponding author; e-mail eva.zazim{at}ueb.cas.cz; fax
420-220390-474.
© 2003 American Society of Plant Biologists
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