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Gene Review

KIF13B  -  kinesin family member 13B

Homo sapiens

Synonyms: GAKIN, KIAA0639, Kinesin-like protein GAKIN, Kinesin-like protein KIF13B
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High impact information on KIF13B

  • Here, we show that the guanylate kinase-like domain of human discs large protein binds directly within the amino acids 607-831 of the stalk domain of GAKIN, a kinesin-like protein of broad distribution [1].
  • Overexpression of green fluorescent protein-fused GAKIN in Madin-Darby canine kidney epithelial cells induced long projections with both GAKIN and endogenous discs large accumulating at the tip of these projections [1].
  • We propose that the GAKIN-hDlg interaction lays the foundation for a general paradigm of coupling MAGUKs to the microtubule-based cytoskeleton, and that this interaction may be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes in vivo [2].
  • Affinity protein purification, peptide sequencing, and cloning of GAKIN cDNA from Jurkat J77 lymphocytes identified GAKIN as a novel member of the kinesin superfamily of motor proteins [2].
  • GAKIN sequence contains a motor domain at the NH(2) terminus, a central stalk domain, and a putative microtubule-interacting sequence called the CAP-Gly domain at the COOH terminus [2].

Biological context of KIF13B

  • We also show that KIF13B and centaurin-alpha(1) colocalize at the leading edges of the cell periphery whereas a deletion mutant of centaurin-alpha(1) that lacks the KIF13B binding site, failed to colocalize with KIF13B in vivo [3].
  • We have recently isolated a novel KIF (kinesin) motor protein (KIF13B) that binds to centaurin-alpha1, an ARF6GAP that binds to the second messenger PIP3 [PtdIns(3,4,5)P3] [4].

Physical interactions of KIF13B

  • Identification of centaurin-alpha1 as a KIF13B interactor suggests that KIF13B may transport ARF6 and/or PIP3 using centaurin-alpha1 as its receptor [4].
  • Centaurin-alpha(1) and KIF13B form a complex in vivo and the KIF13B interaction appears to be specific to centaurin-alpha(1) as other members of the ARF GAP family did not show any binding activity [3].
  • Here we show that a novel protein termed GAKIN binds to the guanylate kinase-like domain of hDlg [2].

Regulatory relationships of KIF13B

  • Finally, we demonstrate that KIF13B binding suppresses the ARF6 GAP activity of centaurin-alpha(1) in intact cells [3].

Other interactions of KIF13B

  • Together, our data suggest a mechanism where direct binding between centaurin-alpha(1) and KIF13B could concentrate centaurin-alpha(1) at the leading edges of cells, thus modulating ARF6 function [3].
  • Neuregulin and KIF13B genes, located within this interval, are interesting functional candidate genes for this HSP form [5].


  1. Direct interaction with a kinesin-related motor mediates transport of mammalian discs large tumor suppressor homologue in epithelial cells. Asaba, N., Hanada, T., Takeuchi, A., Chishti, A.H. J. Biol. Chem. (2003) [Pubmed]
  2. GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes. Hanada, T., Lin, L., Tibaldi, E.V., Reinherz, E.L., Chishti, A.H. J. Biol. Chem. (2000) [Pubmed]
  3. Centaurin-alpha1 interacts directly with kinesin motor protein KIF13B. Venkateswarlu, K., Hanada, T., Chishti, A.H. J. Cell. Sci. (2005) [Pubmed]
  4. Centaurin-alpha1 and KIF13B kinesin motor protein interaction in ARF6 signalling. Kanamarlapudi, V. Biochem. Soc. Trans. (2005) [Pubmed]
  5. A novel locus for hereditary spastic paraplegia with thin corpus callosum and epilepsy. Al-Yahyaee, S., Al-Gazali, L.I., De Jonghe, P., Al-Barwany, H., Al-Kindi, M., De Vriendt, E., Chand, P., Koul, R., Jacob, P.C., Gururaj, A., Sztriha, L., Parrado, A., Van Broeckhoven, C., Bayoumi, R.A. Neurology (2006) [Pubmed]
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