Most UNC-104/KIF1 kinesins are monomeric motors that transport membrane-bou
nded organelles toward the plus ends of microtubules. Recent evidence impli
es that KIF1A, a synaptic vesicle motor, moves processively. This surprisin
g behavior for a monomeric motor depends upon a lysine-rich loop in KIF1A t
hat binds to the negatively charged carboxyl terminus of tubulin and, in th
e context of motor processivity, compensates for the lack of a second motor
domain on the KIF1A holoenzyme.