Kinesin-2 is a heterotrimer

Stable Identifier
Reaction [binding]
Mus musculus
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
7559760 KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport

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

J Cell Biol 1995
8710890 Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B

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

Proc Natl Acad Sci U S A 1996
8232586 Novel heterotrimeric kinesin-related protein purified from sea urchin eggs

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

Nature 1993
Orthologous Events
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