Kinesins bind microtubules

Stable Identifier
Reaction [binding]
Homo sapiens
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All kinesins contain a motor domain or head, the position varies but it is structurally highly conserved (Kull et al. 1996, Sablin et al. 1996). The microtubule-binding site includes structural elements which interact with tubulin and undergo movement between the ADP and ATP bound states. The highly conserved switch I (SSRSH) and II (DLAGSE) motifs, which change in conformation during the ATP hydrolysis cycle, form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).
Literature References
PubMed ID Title Journal Year
2522352 A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses

Goldstein, LS, Yang, JT, Laymon, RA

Cell 1989
2521221 Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities

Rothwell, SW, Murphy, DB, Vaisberg, YA, Kuznetsov, SA, Gelfand, VI

J Biol Chem 1989
1607388 Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells

Vale, RD, McCaffrey, G, Navone, F, Niclas, J, Sparks, L, Hom-Booher, N, Bernstein, HD

J Cell Biol 1992
19116309 Kinesin-14 family proteins HSET/XCTK2 control spindle length by cross-linking and sliding microtubules

Cai, S, Weaver, LN, Ems-McClung, SC, Walczak, CE

Mol Biol Cell 2009
7929562 A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally

Okada, Y, Kondo, S, Noda, Y, Aizawa, H, Sekine, Y, Hirokawa, N, Takemura, R

J Cell Biol 1994
15326200 Human chromokinesin KIF4A functions in chromosome condensation and segregation

Sundareshan, S, Mazumdar, M, Misteli, T

J Cell Biol 2004
16262723 Kinesin-2 is a motor for late endosomes and lysosomes

Schroer, TA, Ginkel, LM, Brown, CL, Vernos, I, Stauber, T, Maier, KC, Wordeman, L

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