Pollen tube microtubules (MTs) are as dynamic as animal MTs and they may in
teract with plasma membrane, endoplasmic reticulum, Golgi apparatus, mitoco
ndria and a variety of cytoplasmic proteins. Bridges connecting MTs to each
other and to membranes have been documented in pollen tubes by electron mi
croscopy; however, the biochemical and molecular nature of these linkages i
s not known. In other cell types interaction between organelles and MTs req
uire the participation of Microtubule-Associated Proteins (MAPs) that bridg
e the cytoskeleton to these organelles. Although biochemical documentation
of such bridging MAPs in plant cells is lacking, it is reasonable to assume
, by analogy with the animal systems, that specialized MAPs regulate MTs po
lymerization and dynamic in pollen tube. As a first step toward testing thi
s hypothesis, the ability of Nicotiana tabacum pollen tube taxol-stabilized
MTs to bind mammalian brain High Molecular Weight MAPs (HMW-MAPs) (MAP2) w
as tested. This association analysis revealed the presence of mammalian MAP
2-binding sites on pollen tube taxol-induced structures suggesting that the
association presumably occurs at conserved domains on the tubulin molecule
s.