Coordinating Synaptic Signaling with CRMP2. (July 2020)

• Record Type: Journal Article
• Authors: Stratton, Harrison; Boinon, Lisa; Moutal, Aubin; Khanna, Rajesh
• Is Part Of: International journal of biochemistry & cell biology. Volume 124(2020)
• Publication Date: 2020-07
• Subjects: Collapsin-response-mediator-protein 2 -- Synaptic signaling -- CaV2.2 -- NaV1.7; Biochemistry -- Periodicals; Cytology -- Periodicals; Biochemistry -- Periodicals; Cell Biology -- Periodicals; Biochimie -- Périodiques; Cytologie -- Périodiques; Biochimie; Cytologie; Biochemistry; Cytology; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); Periodicals; 572.05
• DOI: 10.1016/j.biocel.2020.105759
• Languages: English
• ISSNs: 1357-2725

Abstract

Highlights: CRMP2 is a modulator of ion channel trafficking and intracellular calcium influx. Synaptic transmission can be modulated by post translational modifications of CRMP2. CRMP2 is involved in significant synaptic signaling at both pre-and postsynaptic terminals. CRMP2 is a potential promising therapeutic target for various neurodegenerative diseases. Abstract: Synaptic transmission is a complex process, dysregulation of which underlies several neurological conditions. Collapsin response mediator protein 2 (CRMP2) is a microtubule associated protein expressed ubiquitously in the central nervous system. Identified initially in the context of Semaphorin 3A (Collapsin) induced growth cone collapse, more recent findings revealed the involvement of CRMP2 in ion channel trafficking, kinesin-dependent axonal transport and maintenance of intracellular calcium homeostasis. CRMP2 is a synaptic protein, expressed at pre- and post-synaptic sites. Interactions with proteins such as N-methyl-D-aspartate receptors, syntaxin1A as well as voltage-gated calcium and sodium channels, suggest that CRMP2 may control both the electrical and chemical components of synaptic transmission. This short review will outline the known synaptic interactions of CRMP2 and illustrate its role in synaptic transmission, thereby introducing CRMP2 as a prospective target for the pathophysiological modulation of aberrant synaptic activity.