Here, we dissect two Kinesin-2 motors - the heterotrimeric KIF3A/B/KAP and the homodimeric OSM-3 - and their regulation. While the OSM-3 motor is autoinhibited by the binding of their tail to their head domains if no cargo is bound, the KIF3A/B/KAP is lacking this classic autoinhibition mechanism. Instead, the two tails are necessary for the binding of the KAP subunit and the full runlength of the motor, respectively, while the processivity of the motor is diminished, when the head domains are dephosphorylated. This shows in vitro how these motors adapted their diverse domains to their respective functions .
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Here, we dissect two Kinesin-2 motors - the heterotrimeric KIF3A/B/KAP and the homodimeric OSM-3 - and their regulation. While the OSM-3 motor is autoinhibited by the binding of their tail to their head domains if no cargo is bound, the KIF3A/B/KAP is lacking this classic autoinhibition mechanism. Instead, the two tails are necessary for the binding of the KAP subunit and the full runlength of the motor, respectively, while the processivity of the motor is diminished, when the head domains are d...
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