Kinesin-2 is a heterotrimer

Stable Identifier
R-MMU-984713
Type
Reaction [binding]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Kinesin-2 is a heterotrimer
Kinesin-2 is a heterotrimer with two different motor subunits and an accessory protein that is believed to interact with the cargo, or possibly regulate motor activity (Marszalek & Goldstein 2002). The motor domain interacts with microtubules and contains the ATPase used to translocate the holoenzyme along the microtubule. The coiled-coil stalk is where the two motor subunits interact with each other to form a stable heterodimer. The tail domains interact with the KAP3 non-motor accessory subunit. Kinesin-2 is a plus-end directed kinesin involved in photoreceptor cell function (Jimeno et al. 2006) and normal steady-state localization of late endosomes/lysosomes (Brown et al. 2005).
Literature References
PubMed ID Title Journal Year
8710890 Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B

Okada, Y, Yamazaki, H, Nakata, T, Hirokawa, N

Proc Natl Acad Sci U S A 1996
7559760 KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport

Okada, Y, Yamazaki, H, Nakata, T, Hirokawa, N

J Cell Biol 1995
8232586 Novel heterotrimeric kinesin-related protein purified from sea urchin eggs

Hall, K, Chinn, SW, Vuong, T, Cole, DG, Scholey, JM, Wedaman, KP

Nature 1993
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Orthologous Events
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