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Glutamatergic Synapses: Molecular Organization, Regulation, and Synaptic Plasticity

Call for Papers

Synapses are highly organized subcellular compartments specializing in synaptic transmission and many forms of synaptic plasticity, such as Hebbian synaptic plasticity (LTP and LTD) and homeostatic synaptic plasticity (synaptic upscaling or downscaling). Glutamate receptors (e.g., NMDA and AMPA subtypes), signaling molecules (kinases, phosphatases, palmitoylases, ubiquitin ligases, etc.), and their scaffolding/targeting proteins constitute essential components in synaptic spines. Efficient signal transduction in spines requires scaffolding proteins which bring signaling molecules in close physical proximity to their effectors, forming a signaling center. Activity-dependent reorganization of signaling molecules to the physical proximity of their effector via trafficking/regulation of their scaffolding proteins is critical for the modification of multiple classes of proteins and in turn is required for normal neural plasticity.

Understanding how signaling molecules are regulated by their scaffolding proteins and other modulators will help elucidate the panoply of mechanisms that underlie synaptic plasticity. Moreover, understanding how this organization is perturbed in different neurological diseases will help identify putative therapeutic pathways to help treat myriad synaptopathies. We invite research as well as review articles on any subjects related to molecular organization and its regulation associated with synapse function and neural plasticity.

Potential topics include but are not limited to the following:

  • Glutamate receptor interacting proteins (AMPAR, NMDAR, and mGluR), for example, TARPs, PSD proteins/SAPs, and Homer/Shank
  • Kinase targeting proteins (CaMKII, PKA, and PKC), for example, CaMKII per se, AKAPS, and RACKs
  • Phosphatase targeting proteins (PP1, PP2A, PP2B, PP2C, and STEP, etc.), for example, spinophilin, neurabin, AKAPs, and regulatory subunits
  • Cytoskeletal proteins involved in vesicle trafficking, for example, myosins and neurofilament proteins
  • Cell adhesion molecules (neuroligin, N-CAM, amyloid precursor protein (APP), etc.)
  • Other regulatory molecules such as 14-3-3 that interacts with functionally diverse proteins at synapses

Authors can submit their manuscripts through the Manuscript Tracking System at http://mts.hindawi.com/submit/journals/np/morsp/.

Submission DeadlineFriday, 15 September 2017
Publication DateFebruary 2018

Papers are published upon acceptance, regardless of the Special Issue publication date.

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