Developer site: The content shown here is test data.

MyEClinic
MyEClinic
Health Dictionary AI Health Chat Find an Online Doctor
A serene Zen garden with raked sand and smooth stones, symbolising clarity and calm

Health Dictionary

Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

Back to skin conditions

KIF15

Introduction

Kinesin family member 15 is a protein that in humans is encoded by the KIF15 gene.[1]

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.[1]

Function

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.[2] KIF15 maintains bipolar microtubule spindle apparatus in dividing cells and shares redundant functions with KIF11.[3] KIF15 is thought to promote spindle assembly by cross-linking and sliding along microtubules creating a separation between centrosomes. HeLa cells depleted of KIF11, with reduced microtubule dynamics, are able to form bipolar spindles from acentrosomal asters in a KIF15 dependent manner.[4][5] Hence, inhibition of KIF15 function will be a vital therapeutic approach in cancer chemotherapy[6].

Function in neurons

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.[7][8] KIF15, together with KIF23 become enriched in dendrites as neurons mature to promote the transport of minus-end distal microtubules into nascent dendrites.[7]

Interactions

Interactions

KIF15 has been shown to interact with TPX2. Both these dimers cooperate to slide along microtubules and maintain bipolar spindles.[9][10]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: Kinesin family member 15”.
  2. ↑ Buster DW, Baird DH, Yu W, Solowska JM, Chauvière M, Mazurek A, Kress M, Baas PW (January 2003). “Expression of the mitotic kinesin Kif15 in postmitotic neurons: implications for neuronal migration and development”. J. Neurocytol. 32 (1): 79–96. doi:10.1023/a:1027332432740. PMID 14618103.
  3. ↑ Vanneste D, Takagi M, Imamoto N, Vernos I (November 2009). “The role of Hklp2 in the stabilization and maintenance of spindle bipolarity”. Curr. Biol. 19 (20): 1712–7. doi:10.1016/j.cub.2009.09.019. PMID 19818619.
  4. ↑ Florian S, Mayer TU (October 2011). “Modulated microtubule dynamics enable Hklp2/Kif15 to assemble bipolar spindles”. Cell Cycle. 10 (20): 3533–44. doi:10.4161/cc.10.20.17817. PMID 22024925.
  5. ↑ Dumont J (January 2012). “Bipolar disorder: kinesin-12 to the rescue”. Cell Cycle. 11 (2): 212–3. doi:10.4161/cc.11.2.18785. PMID 22214669.
  6. ↑ Sebastian, Jomon. “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.
  7. ↑ 7.0 7.1 Lin S, Liu M, Mozgova OI, Yu W, Baas PW (October 2012). “Mitotic motors coregulate microtubule patterns in axons and dendrites”. J. Neurosci. 32 (40): 14033–49. doi:10.1523/JNEUROSCI.3070-12.2012. PMC 3482493. PMID 23035110.
  8. ↑ Liu M, Nadar VC, Kozielski F, Kozlowska M, Yu W, Baas PW (November 2010). “Kinesin-12, a mitotic microtubule-associated motor protein, impacts axonal growth, navigation, and branching”. J. Neurosci. 30 (44): 14896–906. doi:10.1523/JNEUROSCI.3739-10.2010. PMC 3064264. PMID 21048148.
  9. ↑ Tanenbaum ME, Macůrek L, Janssen A, Geers EF, Alvarez-Fernández M, Medema RH (November 2009). “Kif15 cooperates with eg5 to promote bipolar spindle assembly”. Curr. Biol. 19 (20): 1703–11. doi:10.1016/j.cub.2009.08.027. PMID 19818618.
  10. ↑ Vanneste D, Ferreira V, Vernos I (October 2011). “Chromokinesins: localization-dependent functions and regulation during cell division”. Biochem. Soc. Trans. 39 (5): 1154–60. doi:10.1042/BST0391154. PMID 21936781.
Further reading

Further reading

External links