The cellular processes of transport, division and, possibly, early dev
elopment all involve microtubule-based motors. Recent work shows that,
unexpectedly, many of these cellular functions are carried out by dif
ferent types of kinesin and kinesin-related motor proteins. The kinesi
n proteins are a large and rapidly growing family of microtubule-motor
proteins that share a 340-amino-acid motor domain. Phylogenetic analy
sis of the conserved motor domains groups the kinesin proteins into a
number of subfamilies, the members of which exhibit a common molecular
organization and related functions. The kinesin proteins that belong
to different subfamilies differ in their rates and polarity of movemen
t along microtubules, and probably in the particles/organelles that th
ey transport. The kinesins arose early in eukaryotic evolution and gen
e duplication has allowed functional specialization to occur, resultin
g in a surprisingly large number of different classes of these protein
s adapted for intracellular transport of vesicles and organelles, and
for assembly and force generation in the meiotic and mitotic spindles.