Kinesin family member 15 is a protein that in humans is encoded by the KIF15 gene.[5]
This gene encodes a motor protein that is part of the kinesin superfamily. KIF15 maintains half spindle separation by opposing forces generated by other motor proteins. KIF15 co-localizes with microtubules and actin filaments in both dividing cells and in postmitotic neurons.[5]
Function
KIF15 (also known as Kinesin-12 and HKLP2) is a motor protein expressed in all cells during mitosis and in postmitotic neurons undergoing axon growth.[6] KIF15 maintains bipolar microtubule spindle apparatus in dividing cells and shares redundant functions with KIF11.[7] KIF15 is thought to promote spindle assembly by cross-linking and sliding along microtubules creating a separation between centrosomes. The microtubule localization of Kif15 is being regulated by Kinesin binding protein (KBP).[8] HeLa cells depleted of KIF11, with reduced microtubule dynamics, are able to form bipolar spindles from acentrosomal asters in a KIF15 dependent manner.[9][10] Hence, inhibition of KIF15 function will be a vital therapeutic approach in cancer chemotherapy.[11] Since KIF11 and KIF15 are functionally redundant, drugs targeting both the proteins will be more potent.[8]
Function in neurons
KIF15 restricts the movement of short microtubules into growing axons by generating forces on microtubules which counteract those generated by cytoplasmic dynein.[12][13] KIF15, together with KIF23 become enriched in dendrites as neurons mature to promote the transport of minus-end distal microtubules into nascent dendrites.[12]
Interactions
KIF15 has been shown to interact with TPX2. Both these dimers cooperate to slide along microtubules and maintain bipolar spindles.[14][15]
^Buster DW, Baird DH, Yu W, Solowska JM, Chauvière M, Mazurek A, et al. (January 2003). "Expression of the mitotic kinesin Kif15 in postmitotic neurons: implications for neuronal migration and development". Journal of Neurocytology. 32 (1): 79–96. doi:10.1023/a:1027332432740. PMID14618103. S2CID6734564.
^ abSebastian J, Rathinasamy K (July 2019). "Benserazide Perturbs Kif15-kinesin Binding Protein Interaction with Prolonged Metaphase and Defects in Chromosomal Congression: A Study Based on in silico Modeling and Cell Culture". Molecular Informatics. 39 (3): minf.201900035. doi:10.1002/minf.201900035. PMID31347789. S2CID198911009.
^Sebastian J (June 2017). "Dihydropyrazole and dihydropyrrole structures based design of Kif15 inhibitors as novel therapeutic agents for cancer". Computational Biology and Chemistry. 68: 164–174. doi:10.1016/j.compbiolchem.2017.03.006. PMID28355588.
