Analysis of the kinesin superfamily: insights into structure and function

Kinesin superfamily proteins (KIFs) are key players or ‘hub’ proteins in the intracellular transport system, which is essential for cellular function and morphology. The KIF superfamily is also the first large protein family in mammals whose constituents have been completely identified and confirmed both in silico and in vivo. Numerous studies have revealed the structures and functions of individual family members; however, the relationships between members or a perspective of the whole superfamily structure until recently remained elusive. Here, we present a comprehensive summary based on a large, systematic phylogenetic analysis of the kinesin superfamily. All available sequences in public databases, including genomic information from all model organisms, were analyzed to yield the most complete phylogenetic kinesin tree thus far, comprising 14 families. This comprehensive classification builds on the recently proposed standardized nomenclature for kinesins and allows systematic analysis of the structural and functional relationships within the kinesin superfamily. Kinesin superfamily proteins (KIFs) are key players or ‘hub’ proteins in the intracellular transport system, which is essential for cellular function and morphology. The KIF superfamily is also the first large protein family in mammals whose constituents have been completely identified and confirmed both in silico and in vivo. Numerous studies have revealed the structures and functions of individual family members; however, the relationships between members or a perspective of the whole superfamily structure until recently remained elusive. Here, we present a comprehensive summary based on a large, systematic phylogenetic analysis of the kinesin superfamily. All available sequences in public databases, including genomic information from all model organisms, were analyzed to yield the most complete phylogenetic kinesin tree thus far, comprising 14 families. This comprehensive classification builds on the recently proposed standardized nomenclature for kinesins and allows systematic analysis of the structural and functional relationships within the kinesin superfamily. a 42–45 amino acid repeat found to be a site of protein–protein interaction. ‘BimC’ (for: ‘Block In Mitosis’), was first identified as a gene that, when mutated, causes cells to remain in mitosis in the filamentous fungus Aspergillus nidulans. A ‘BimC box’ refers to a motif that is highly conserved in Kinesin-5 and is a recognition and phosphorylation site for p34/Cdc42 (also see text). during cytokinesis in higher plants, the cell wall between daughter cells is created by the maturation of a disk-shaped structure called the cell plate. The cell plate is formed by active microtubule-dependent organelle transport based on the phragmoplast, a scaffold consisting mainly of microtubules and microfilaments. the preprophase band is formed during G2 and prophase of the cell cycle and marks where the cell plate will form. It is generally a circular bundle of microtubules associated with actin filaments and other proteins. Active vesicle transport is observed along the preprophase band. during interphase, relatively short and overlapping microtubules come in close contact with the plasma membrane. This cortical array or cortical microtubule array coordinates morphogenesis by controlling the direction of cell growth, the location of divisional planes and local wall in-growth. kinesin-like calmodulin-binding proteins (KCBPs) have catalytic core domains at the C-terminus of the molecule and posses a calmodulin-binding motif in the catalytic core. Members of this subfamily have been shown to have calmodulin-binding properties through the calmodulin-binding motif.