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Abelson phosphorylation of CLASP2 modulates its association with microtubules and actin

The Abelson (Abl) non-receptor tyrosine kinase regulates the cytoskeleton during multiple stages of neural development, from neurulation, to the articulation of axons and dendrites, to synapse formation and maintenance. We previously showed that Abl is genetically linked to the microtubule (MT) plus...

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Bibliographic Details
Main Author: Engel, Ulrike (Author)
Format: Article (Journal)
Language:English
Published: 12 March 2014
In: Cytoskeleton
Year: 2014, Volume: 71, Issue: 3, Pages: 195-209
ISSN:1949-3592
DOI:10.1002/cm.21164
Online Access:Verlag, kostenfrei registrierungspflichtig, Volltext: http://dx.doi.org/10.1002/cm.21164
Verlag, kostenfrei registrierungspflichtig, Volltext: http://onlinelibrary.wiley.com/doi/10.1002/cm.21164/abstract
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Author Notes:Ulrike Engel, Yougen Zhan, Jennifer B. Long, Scott N. Boyle, Bryan A. Ballif, Karel Dorey, Steven P. Gygi, Anthony J. Koleske, and David VanVactor

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520 |a The Abelson (Abl) non-receptor tyrosine kinase regulates the cytoskeleton during multiple stages of neural development, from neurulation, to the articulation of axons and dendrites, to synapse formation and maintenance. We previously showed that Abl is genetically linked to the microtubule (MT) plus end tracking protein (+TIP) CLASP in Drosophila. Here we show in vertebrate cells that Abl binds to CLASP and phosphorylates it in response to serum or PDGF stimulation. In vitro, Abl phosphorylates CLASP with a Km of 1.89 µM, indicating that CLASP is a bona fide substrate. Abl-phosphorylated tyrosine residues that we detect in CLASP by mass spectrometry lie within previously mapped F-actin and MT plus end interaction domains. Using purified proteins, we find that Abl phosphorylation modulates direct binding between purified CLASP2 with both MTs and actin. Consistent with these observations, Abl-induced phosphorylation of CLASP2 modulates its localization as well as the distribution of F-actin structures in spinal cord growth cones. Our data suggest that the functional relationship between Abl and CLASP2 is conserved and provides a means to control the CLASP2 association with the cytoskeleton. 
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