Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions

Aubin Moutal, Katherine A. White, Aude Chefdeville, Rachel N. Laufmann, Peter F. Vitiello, Douglas Feinstein, Jill M. Weimer, Rajesh Khanna

Research output: Contribution to journalReview article

3 Citations (Scopus)

Abstract

Collapsin response mediator proteins (CRMPs) are a family of ubiquitously expressed, homologous phosphoproteins best known for coordinating cytoskeletal formation and regulating cellular division, migration, polarity, and synaptic connection. CRMP2, the most studied of the five family members, is best known for its affinity for tubulin heterodimers and function in regulating the microtubule network. These functions are tightly regulated by post-translational modifications including phosphorylation, SUMOylation, oxidation, and O-GlcNAcylation. While CRMP2’s physiological functions rely mostly on its non-phosphorylated state, dysregulation of CRMP2 phosphorylation and SUMOylation has been reported to be involved in the pathophysiology of multiple diseases including cancer, chronic pain, spinal cord injury, neurofibromatosis type 1, and others. Here, we provide a consolidated update on what is known about CRMP2 signaling and function, first focusing on axonal growth and neuronal polarity, then illustrating the link between dysregulated CRMP2 post-translational modifications and diseases. We additionally discuss the roles of CRMP2 in non-neuronal cells, both in the CNS and regions of the periphery. Finally, we offer thoughts on the therapeutic implications of modulating CRMP2 function in a variety of diseases.

Original languageEnglish (US)
Pages (from-to)6736-6755
Number of pages20
JournalMolecular Neurobiology
Volume56
Issue number10
DOIs
StatePublished - Oct 1 2019

Fingerprint

Post Translational Protein Processing
Sumoylation
Semaphorin-3A
Phosphorylation
Neurofibromatosis 1
Phosphoproteins
Tubulin
Spinal Cord Injuries
Microtubules
Chronic Pain
Growth
Drive
Proteins
Therapeutics

Keywords

  • Alzheimer’s disease
  • Cancer
  • Chronic pain
  • CRMP2
  • Human disease
  • Interactome
  • Multiple sclerosis
  • Neurite outgrowth
  • Non-neuronal cells
  • Post-translational modifications
  • Stroke
  • Therapeutics

ASJC Scopus subject areas

  • Neuroscience (miscellaneous)
  • Neurology
  • Cellular and Molecular Neuroscience

Cite this

Moutal, A., White, K. A., Chefdeville, A., Laufmann, R. N., Vitiello, P. F., Feinstein, D., ... Khanna, R. (2019). Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions. Molecular Neurobiology, 56(10), 6736-6755. https://doi.org/10.1007/s12035-019-1568-4

Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions. / Moutal, Aubin; White, Katherine A.; Chefdeville, Aude; Laufmann, Rachel N.; Vitiello, Peter F.; Feinstein, Douglas; Weimer, Jill M.; Khanna, Rajesh.

In: Molecular Neurobiology, Vol. 56, No. 10, 01.10.2019, p. 6736-6755.

Research output: Contribution to journalReview article

Moutal, A, White, KA, Chefdeville, A, Laufmann, RN, Vitiello, PF, Feinstein, D, Weimer, JM & Khanna, R 2019, 'Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions', Molecular Neurobiology, vol. 56, no. 10, pp. 6736-6755. https://doi.org/10.1007/s12035-019-1568-4
Moutal A, White KA, Chefdeville A, Laufmann RN, Vitiello PF, Feinstein D et al. Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions. Molecular Neurobiology. 2019 Oct 1;56(10):6736-6755. https://doi.org/10.1007/s12035-019-1568-4
Moutal, Aubin ; White, Katherine A. ; Chefdeville, Aude ; Laufmann, Rachel N. ; Vitiello, Peter F. ; Feinstein, Douglas ; Weimer, Jill M. ; Khanna, Rajesh. / Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions. In: Molecular Neurobiology. 2019 ; Vol. 56, No. 10. pp. 6736-6755.
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