Kinesin-2: A family of heterotrimeric and homodimeric motors with diverse intracellular transport functions

Jonathan M. Scholey

Research output: Contribution to journalArticlepeer-review

93 Scopus citations


Kinesin-2 was first purified as a heterotrimeric, anterograde, microtubule-based motor consisting of two distinct kinesin-related subunits and a novel associated protein (KAP) that is currently best known for its role in intraflagellar transport and ciliogenesis. Subsequent work, however, has revealed diversity in the oligomeric state of different kinesin-2 motors owing to the combinatorial heterodimerization of its subunits and the coexistence of both heterotrimeric and homodimeric kinesin-2 motors in some cells. Although the functional significance of the homo- versus heteromeric organization of kinesin-2 motor subunits and the role of KAP remain uncertain, functional studies suggest that cooperation between different types of kinesin-2 motors or between kinesin-2 and a member of a different motor family can generate diverse patterns of anterograde intracellular transport. Moreover, despite being restricted to ciliated eukaryotes, kinesin-2 motors are now known to drive diverse transport events outside cilia. Here, I review the organization, assembly, phylogeny, biological functions, and motility mechanism of this diverse family of intracellular transport motors.

Original languageEnglish (US)
Pages (from-to)443-469
Number of pages27
JournalAnnual Review of Cell and Developmental Biology
StatePublished - Oct 2013


  • cilium biogenesis
  • heterotrimeric kinesin-2
  • homodimeric kinesin-2
  • intracellular transport
  • microtubule-based motor proteins

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology
  • Medicine(all)


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