| Annotated protein: | Kinesin-like protein KIF3A (Microtubule plus end-directed kinesin motor 3A). Gene symbol: KIF3A. Taxonomy: Mus musculus (Mouse). Uniprot ID: P28741 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ KIF3A |
| Ontology domain: | Cellular Component |
| SynGO term: | postsynapse (GO:0098794) |
| Synapse type(s): | hippocampus |
| Annotated paper: | Ichinose S, et al. "Mechanism of Activity-Dependent Cargo Loading via the Phosphorylation of KIF3A by PKA and CaMKIIa" Neuron. 2015 Sep 2;87(5):1022-35 PMID:26335646 |
| Figure(s): | Figure 1-8 |
| Annotation description: | "KIF3, a member of the kinesin-2 family, forms a heterotrimeric complex that consists of KIF3A, KIF3B, and kinesin-associated protein 3 (KAP3) (Kondo et al., 1994, Teng et al., 2005, Yamazaki et al., 1996)." Authors show that KIF3A is involved in the transport of N-cadherin (Cadherin-2, gene CDH2), a synaptic adhesion molecule, to dendritic spines. Because authors show the KIF3A+KIF3B+KAP3 complex delivers N-cadherin to the postsynapse, postsynaptic localization is implied. This is also shown in PMID:31746486, where the same complex is shown to transport NR2 to the PSD and high resolution imaging shows KIF3B at the postsynapse. Highlights section; - The cargo-bound KIF3A was phosphorylated by specific kinases, PKA and CaMKIIa. - Phosphorylation of the KIF3A upregulates the loading and transport of N-cadherin. - N-cadherin was accumulating in the spine during homeostatic plasticity. - Phospho-KIF3A enhances the N-cadherin accumulation during homeostatic plasticity. |
| Evidence tracking, Biological System: | Intact tissue Cultured neurons |
| Evidence tracking, Protein Targeting: | Over-expression Antagonist / agonist Antibody (detection) |
| Evidence tracking, Experiment Assay: | Confocal IP + WB/MSMS Western blot |
| Non-tracable Author Statement (NAS): | This annotation required some inference over additional information/literature, and is not solely based on observations made in the annotated paper by its original authors. |
| Annotator(s): | Frank Koopmans (ORCID:0000-0002-4973-5732) Guus Smit (ORCID:0000-0002-2286-1587) Matthijs Verhage (ORCID:0000-0002-2514-0216) |
| Lab: | Department of Functional Genomics, Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands |
| Additional literature: | biochemical characterization of KIF3A/B/C in rat brain. @ PMID:9487132 immunoprecipitations in mouse brain lysate show KIF3C associates with KIF3A, but not KIF3B. Also shows KIF3B/C in synaptic biochemical fractions and microtubule binding characteristics of KIF3C @ PMID:9450952 KIF3A/B are enriched in the same synaptic biochemical fractions prepared from mouse brain. KIF3A and KIF3B form a heterodimer in vitro that provides plus end--directed motor activity. The KIF3 complex Is a heterotrimeric motor in vivo. @ PMID:7559760 "Here we characterized a new member of the kinesin superfamily, KIF3A (50-nm rod with globular head and tail), and found that it is localized in neurons, associated with membrane organdie fractions, and accumulates with anterogradely moving membrane organelles after ligation of peripheral nerves. Furthermore, native KIF3A (a complex of 80/85 KIF3A heavy chain and a 95-kD polypeptide) revealed microtubule gliding activity and baculovirus-expressed KIF3A heavy chain demonstrated microtubule plus end-directed (anterograde) motility in vitro" @ PMID:7515068 "Immunocytochemistry using cultured hippocampal neurons of Kif3b+/+ mice showed that KIF3B puncta were colocalized with APC and NR2A in dendritic shafts (Fig 1D) and in PSD95-positive spines (Fig 1E)." @ PMID:31746486 |
| SynGO annotation ID: | 5445 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |