Kinesin-1 (previously referred to as conventional kinesin, kinesin heavy chain or KHC) is a mechanochemical protein capable of utilizing chemical energy from ATP hydrolysis to generate mechanical force. In the presence of ATP, Kinesin-1 can bind to and move on microtubules (see Motility). The ability to translocate along the microtubule lattice has led to the classification of Kinesin-1 as a microtubule motor protein. Kinesin-1 is unrelated in sequence to the other known class of microtubule motor proteins, the dyneins, and is thought to perform functions in the cell distinct from the dyneins.
The mechanism by which molecular motor proteins convert energy from ATP hydrolysis into mechanical force is not known. A problem related to their mechanism of function is the molecular basis of polarity of translocation along the microtubule: some kinesin motors move toward microtubule minus, instead of plus ends like Kinesin-1. The coupling of the ATPase cycle to force generation and the determinants of motor polarity are actively being investigated using biochemical, biophysical, and molecular approaches. Other areas of investigation include the regulation of Kinesin-1 function in the cell and identification of proteins that enable Kinesin-1 to interact with intracellular vesicles and organelles.
Recent Reviews
Howard, J. (1996) Ann. Rev. Physiol. 58, 703-729
Vallee, R.B. & Sheetz, M.P. (1996) Sci. 271, 1539-1544
Bloom, G.S. & Endow, S.A. (1995) Prot. Profile 2, 1109-1171
Pereira, A. & Goldstein, L.S.B. (1994) In Microtubules (ed. J.S. Hyams & C.W. Lloyd) pp 269-284, Wiley-Liss, NY
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Copyright 1996-2005. All rights reserved.
Created 7 July 1996 20:00 GMT
Modified 20 February 2020 17:45 GMT
