RGD Reference Report - Mammalian Kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Mammalian Kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition.

Authors: Hammond, Jennetta W  Cai, Dawen  Blasius, T Lynne  Li, Zhe  Jiang, Yuyang  Jih, Gloria T  Meyhofer, Edgar  Verhey, Kristen J 
Citation: Hammond JW, etal., PLoS Biol. 2009 Mar 31;7(3):e72. doi: 10.1371/journal.pbio.1000072.
RGD ID: 12914798
Pubmed: PMID:19338388   (View Abstract at PubMed)
PMCID: PMC2661964   (View Article at PubMed Central)
DOI: DOI:10.1371/journal.pbio.1000072   (Journal Full-text)

Kinesin-3 motors drive the transport of synaptic vesicles and other membrane-bound organelles in neuronal cells. In the absence of cargo, kinesin motors are kept inactive to prevent motility and ATP hydrolysis. Current models state that the Kinesin-3 motor KIF1A is monomeric in the inactive state and that activation results from concentration-driven dimerization on the cargo membrane. To test this model, we have examined the activity and dimerization state of KIF1A. Unexpectedly, we found that both native and expressed proteins are dimeric in the inactive state. Thus, KIF1A motors are not activated by cargo-induced dimerization. Rather, we show that KIF1A motors are autoinhibited by two distinct inhibitory mechanisms, suggesting a simple model for activation of dimeric KIF1A motors by cargo binding. Successive truncations result in monomeric and dimeric motors that can undergo one-dimensional diffusion along the microtubule lattice. However, only dimeric motors undergo ATP-dependent processive motility. Thus, KIF1A may be uniquely suited to use both diffuse and processive motility to drive long-distance transport in neuronal cells.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein transport along microtubule  IDA 12914798 RGD 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
neuronal cell body  IDA 12914798 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding enablesIPIUniProtKB:A0A8I6A6V512914798PMID:19338388IntAct 
identical protein binding  IPIKif1a (Rattus norvegicus)12914798homodimerizationRGD 
microtubule binding  IDA 12914798 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Kif1a  (kinesin family member 1A)


Additional Information