Kinesin light chains

Morfini, G., Szebenyi, G., Elluru, R., Ratner, N. and Brady, S. T. Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 23 281-293, 2002. 

Stenoien, D. S. and Brady, S. T. Immunochemical analysis of kinesin light chain function. Molec. Biol. Cell 8 675-689, 1997. 

The axonal transport of APP in neurons is mediated by the direct binding of APP to the kinesin light chain subunit of kinesin I. An axonal membrane compartment contains APP, P-secretase, and PSl, and the fast anterograde axonal transport of this compartment is mediated by APP and kinesin I. APP proteolysis in this... 

The question of how DnaJ proteins interact with substrates and mediate their transfer onto Hsp70 partner proteins is not answered for any of the three classes of DnaJ proteins. Some DnaJ homologs have broad substrate specificity, such as E. coli DnaJ and yeast Ydjl, while others have more restricted substrate spectra. In particular the DnaJ proteins of class III may either bind a restricted number of substrates, such as the clathrin-specific auxilin or the kinesin light chain, or they may not bind substrates themselves but rather are positioned in close proximity to substrates. The latter seems to be the case for Dj 1A in the plasma membrane of E. coli (Clarke et al, 1997 Kelley and Georgopoulos, 1997a), Sec63 at the translocation pore in the ER (Corsi and Schekman, 1996 Rapoport et al., 1996), and cysteine string proteins on the surface of neurosecretory vesicles (Buchner and Bundersen, 1997). 

Kamal, A., Stokin, G.B., Yang, Z., Xia, C.H. and Goldstein, L.S. 2000. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28 449-459... 

In neurons and non-neuronal cells, kinesin is associated with a variety of MBOs, ranging from synaptic vesicles to mitochondria to lysosomes. In addition to its role in fast axonal transport and related phenomena in non-neuronal cells, kinesin appears to be involved in constitutive cycling of membranes between the Golgi and endoplasmic reticulum. However, kinesin is not associated with all cellular membranes. For example, the nucleus, membranes of the Golgi complex and the plasma membrane all appear to lack kinesin. Kinesin interactions with membranes are thought to involve the light chains and carboxyl termini of heavy chains. However, neither this selectivity nor the molecular basis for binding of kinesin and other motors to membranes is well understood. 

Pfister, K. K., Wagner, M. C., Stenoien, D., Bloom, G. S. and Brady, S. T9. Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells. /. Cell Biol. 108 1453-1463, 1989. 

Avsiuk, A., Minin, A., and Gyoeva, F. (1995). Kinesin associated wth vimentin intermediate filaments contains a specific light chain. Doklady Biol. Sci. 345, 644-646. 

Kinesin-1 comprises three major domains the N-terminal motor domain that can be subdivided into the core motor domain and the adjacent neck linker and neck region, the central stalk domain, and the C-terminal tail or light chain-binding domain (Fig. 1A). The core motor domain has a length of about 325 amino acids and contains both the microtubule and the nucleotide binding elements. In different kinesin families, this motor... 

Fig. 1. Domain structures of typical members of the kinesin superfamily. (A) Bar diagram of the kinesin heavy chain (KHC) of conventional kinesin (kinesin-1 family) as a typical representative of N-type motors (motor domain at the N-terminus, red) the cartoon model beneath the bar diagram shows the tetrameric complex of two heavy and two light chains. (B) M-type kinesin like MCAK of the kinesin-13 family. (C) C-type kinesin like Ned of the kinesin-14 family.

Figure 34.7. Kinesin at Low Resolution. An electron micrograph of conventional kinesin reveals an elongated structure with two heads at one end. The position of the light chains was confirmed through the use of antibody labels. [After N. Hirokawa, K. K. Pfister, H. Yorifuji, M. C. Wagner, S. T. Brady, and G. S. Broom. Cell 56 (1989) 867.]...

Kinesins (20) ATP Eleavy and light chains head domains with ATPase activity and microtubule-binding site Cytoplasm Transport of cargo vesicles and chromosomes during mitosis... 

A sequence called the tetratrico peptide sequence has been recently identified in the light chains of kinesin I and may interact with receptor proteins in the membrane of various cargoes. Such interactions would tether the cargo organelle or vesicle to kinesin. For instance, the tetratrico peptide sequence has been found to bind to several proteins, including the amyloid precursor protein. Other kinesins may have different interaction sequences that bind to other receptors on membranes. 

Fig 2.9. The microtubular motors dynein and kinesin can attach to organelles with their light chains and then use energy from ATP to walk along the microtubule. Dynein walks towards the minus end and kinesin walks towards the plus end of the microtubules. 

Kinesins mediate anterograde transport in a variety of organisms and tissues. Since its discovery, much has been learned about the biochemical, pharmacological and molecular properties of kinesin [44, 45], Kinesin is the most abundant member of the kinesin family in vertebrates and is widely distributed in neuronal and nonneuronal cells. The holoenzyme is a heterotetramer comprising two heavy chains (115-130 kDa) and two light... 

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