Introduction to the Kinesin Superfamily

The kinesins are a superfamily of proteins that interact with the microtubule cytoskeleton. Kinesins use the turnover of ATP to regulate their interaction with microtubules. The first kinesin was discovered in 1985 as a soluble protein that supported ATP-dependent movement of purified microtubules. The conserved kinesin motor domain consists of ~350 amino acids and contains both the nucleotide-binding site and the microtubule-binding interface. The kinesin motor domain acts as a nucleotide-gated switch, with its conformation dependent on nucleotide status. Whilst the rules defining distinct families and their associated nomenclature have not changed, the increase in available genome sequences from a greater diversity of organisms and advancements in phylogenetic methods have permitted more sophisticated and inclusive analyses of kinesin repertoires. The chapter presents an overview of the key concepts discussed in this book. The book discusses the individual families that comprise the kinesin superfamily.