Insights into the activation of Kinesin1 from the molecular characterisation of JIP3/4 binding to Kif5b

Fernando Vilela (1, 2) , Mélanie Chenon (1, 3) , Christophe Velours (4, 1) , Jessica Andreani (1) , Paola Llinas (1) , Julie Ménétrey (1)

1 I2BC - Institut de Biologie Intégrative de la Cellule
2 Imagerie structurale - Structural Image Analysis
3 CBM - Centre de biophysique moléculaire
4 MFP - Microbiologie Fondamentale et Pathogénicité

Abstract Whereas our understanding of kinesin auto-inhibition mechanisms is improving faster, important insights into kinesin activation mechanisms such as those controlled by cargo-motor adaptors are still missing. JIP3 and JIP4 are versatile motor-cargo adaptors for kinesin1 and dynein-dynactin motors enabling bi-directional transport on microtubules. JIP3 activates kinesin1 heavy chains, independently of kinesin1 light chains. In this report, we characterize the molecular details of the binding of the kinesin1 heavy chain, Kif5b to the motor-cargo adaptors, JIP3 and JIP4, using biophysical approaches. The definition of the exact binding site of Kif5b, as well as the specificity of interaction between JIP3 and JIP4 provide new insights into kinesin1 activation.

Mots clés: Kinesin1; Regulation; motor adaptor; JIP3; RH1 domain

Domaines: Sciences du Vivant [q-bio]

Fernando Vilela, Mélanie Chenon, Christophe Velours, Jessica Andreani, Paola Llinas, et al.. Insights into the activation of Kinesin1 from the molecular characterisation of JIP3/4 binding to Kif5b. 2022. ⟨hal-04301953⟩