Dyneins
Dyneins
There are two types of microtubule motor proteins these are kinesins and dyneins. They have globular heads which bind to the microtubule and also bind ATP. The hydrolysis of ATP is what drives movement. The tail regions of the motor proteins bind the cargo e.g. endoplasmic reticulum, Golgi apparatus. The dyneins are a family of minus-end-directed microtubule motors, whereas kinesins are plus-end-directed motors (Alberts et al. 2008:1014). Dyneins are composed of two or three heavy chains and a large variable number of associated intermediate and light chains (Alberts et al. 2008:1014). The dyneins family consists of two major branches, cytoplasmic dynein and axonemal dynein (Alberts et al. 2008:1014).
Cytoplasmic Dynein
Cytoplasmic dynein is typically composed of heavy chain homodimers, with two large motor domains as heads (Alberts et al. 2008:1014). These are found in probably all eukaryotic cells as they are important for vesicle trafficking and for the localization of the Golgi apparatus near to the centre of the cell (Alberts et al. 2008:1014-1015). Cytoplasmic dynein has molecular mass of about 1.5 Megadaltons (Wikipedia.2011). Cytoplasmic dynein transports its cargo by “walking” along the microtubule without becoming detached (Wikipedia.2011).
Axonemal dyneins
Axonemal dynein includes heterodimers, two motor-domain heads, and heterotrimers, three motor-domain heads (Alberts et al. 2008:1015). These are highly specialised for sliding movements of microtubules that drive the beating of cilia and flagella (Alberts et al. 2008:1015). In a test tube axonemal dyneins can move microtubules at a rate of 14µm/sec (Alberts et al. 2008:1015). This is far faster than kinesins which are only able to move at speeds of around 2-3µm/sec (Alberts et al. 2008:1015).
References
Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008) Molecular Biology of the cell, fifth edition, New York: Garland Science.
Wikipedia (2011) Dynein [Online] Available at: http://en.wikipedia.org/wiki/Dynein ( last accessed 28.11.2011).