Reactome | Kinesins move along microtubules consuming ATP

Kinesins move along microtubules consuming ATP

Stable Identifier

R-HSA-983259

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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Kinesins move along microtubules consuming ATP

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Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These 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 by cryo-electron microscopy in human conventional kinesin (Sindelar & Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).

Literature References

PubMed ID	Title	Journal	Year
2142332	Evidence that the head of kinesin is sufficient for force generation and motility in vitro Yang, JT, Saxton, WM, Stewart, RJ, Raff, EC, Goldstein, LS	Science	1990
8602245	Direct observation of single kinesin molecules moving along microtubules Vale, RD, Funatsu, T, Pierce, DW, Romberg, L, Harada, Y, Yanagida, T	Nature	1996
12368902	Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy Sindelar, CV, Budny, MJ, Rice, S, Naber, N, Fletterick, R, Cooke, R	Nat Struct Biol	2002