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RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system.

Publication ,  Journal Article
Cho, K-I; Yi, H; Desai, R; Hand, AR; Haas, AL; Ferreira, PA
Published in: EMBO Rep
May 2009

The association of cargoes to kinesins is thought to promote kinesin activation, yet the validation of such a model with native cargoes is lacking because none is known to activate kinesins directly in an in vitro system of purified components. The RAN-binding protein 2 (RANBP2), through its kinesin-binding domain (KBD), associates in vivo with kinesin-1, KIF5B/KIF5C. Here, we show that KBD and its flanking domains, RAN GTPase-binding domains 2 and 3 (RBD2/RBD3), activate the ATPase activity of KIF5B approximately 30-fold in the presence of microtubules and ATP. The activation kinetics of KIF5B by RANBP2 is biphasic and highly cooperative. Deletion of one of its RBDs lowers the activation of KIF5B threefold and abolishes cooperativity. Remarkably, RBD2-KBD-RBD3 induces unfolding and modest activation of KIF5B in the absence of microtubules. Hence, RANBP2 is the first native and positive allosteric activator known to jump-start and boost directly the activity of a kinesin.

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Published In

EMBO Rep

DOI

EISSN

1469-3178

Publication Date

May 2009

Volume

10

Issue

5

Start / End Page

480 / 486

Location

England

Related Subject Headings

  • Protein Structure, Tertiary
  • Protein Binding
  • Nuclear Pore Complex Proteins
  • Molecular Chaperones
  • Models, Biological
  • Microtubules
  • Kinetics
  • Kinesins
  • Humans
  • Developmental Biology
 

Citation

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Cho, K.-I., Yi, H., Desai, R., Hand, A. R., Haas, A. L., & Ferreira, P. A. (2009). RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO Rep, 10(5), 480–486. https://doi.org/10.1038/embor.2009.29
Cho, Kyoung-in, Haiqing Yi, Ria Desai, Arthur R. Hand, Arthur L. Haas, and Paulo A. Ferreira. “RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system.EMBO Rep 10, no. 5 (May 2009): 480–86. https://doi.org/10.1038/embor.2009.29.
Cho K-I, Yi H, Desai R, Hand AR, Haas AL, Ferreira PA. RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO Rep. 2009 May;10(5):480–6.
Cho, Kyoung-in, et al. “RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system.EMBO Rep, vol. 10, no. 5, May 2009, pp. 480–86. Pubmed, doi:10.1038/embor.2009.29.
Cho K-I, Yi H, Desai R, Hand AR, Haas AL, Ferreira PA. RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO Rep. 2009 May;10(5):480–486.
Journal cover image

Published In

EMBO Rep

DOI

EISSN

1469-3178

Publication Date

May 2009

Volume

10

Issue

5

Start / End Page

480 / 486

Location

England

Related Subject Headings

  • Protein Structure, Tertiary
  • Protein Binding
  • Nuclear Pore Complex Proteins
  • Molecular Chaperones
  • Models, Biological
  • Microtubules
  • Kinetics
  • Kinesins
  • Humans
  • Developmental Biology