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Literature summary for 3.6.4.B1 extracted from

  • Cho, K.I.; Cai, Y.; Yi, H.; Yeh, A.; Aslanukov, A.; Ferreira, P.A.
    Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function (2007), Traffic, 8, 1722-1735.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in ganglion RGC-5 neurons and NIH3T3 fibroblast cells Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the selection of a large array of cargoes for transport by a restricted number of kinesin motor proteins is mediated by adaptor proteins such as Ran-binding protein 2 ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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isoforms KIF5A, KIF5B, KIF5C
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the selection of a large array of cargoes for transport by a restricted number of kinesin motor proteins is mediated by adaptor proteins such as Ran-binding protein 2 Homo sapiens ?
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?

Subunits

Subunits Comment Organism
More Ran-binding protein 2 associates selectively with kinesins KIF5B and KIF5C, but not KIF5A. A single residue conserved in KIF5B and KIF5C, but not KIF5A, confers KIF5-isotype-specific association with RanBP2. Interaction is also mediated by a conserved leucine-like heptad motif present in KIF5s and KBD of RanBP2. Selective inhibition of the interaction between kinesin-bindiing domain of RanBP2 and KIF5B/KIF5C in cell lines causes perinuclear clustering of mitochondria, but not of lysosomes, deficits inmitochondrialmembrane potential and cell shrinkage Homo sapiens