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Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders

Protein phosphorylation and dephosphorylation are two essential and vital cellular mechanisms that regulate many receptors and enzymes through kinases and phosphatases. Ca(2+)- dependent kinases and phosphatases are responsible for controlling neuronal processing; balance is achieved through opposit...

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Autores principales: Khan, Raheel, Kulasiri, Don, Samarasinghe, Sandhya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Wolters Kluwer - Medknow 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8224123/
https://www.ncbi.nlm.nih.gov/pubmed/33269764
http://dx.doi.org/10.4103/1673-5374.300331
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author Khan, Raheel
Kulasiri, Don
Samarasinghe, Sandhya
author_facet Khan, Raheel
Kulasiri, Don
Samarasinghe, Sandhya
author_sort Khan, Raheel
collection PubMed
description Protein phosphorylation and dephosphorylation are two essential and vital cellular mechanisms that regulate many receptors and enzymes through kinases and phosphatases. Ca(2+)- dependent kinases and phosphatases are responsible for controlling neuronal processing; balance is achieved through opposition. During molecular mechanisms of learning and memory, kinases generally modulate positively while phosphatases modulate negatively. This review outlines some of the critical physiological and structural aspects of kinases and phosphatases involved in maintaining postsynaptic structural plasticity. It also explores the link between neuronal disorders and the deregulation of phosphatases and kinases.
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spelling pubmed-82241232021-07-02 Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders Khan, Raheel Kulasiri, Don Samarasinghe, Sandhya Neural Regen Res Review Protein phosphorylation and dephosphorylation are two essential and vital cellular mechanisms that regulate many receptors and enzymes through kinases and phosphatases. Ca(2+)- dependent kinases and phosphatases are responsible for controlling neuronal processing; balance is achieved through opposition. During molecular mechanisms of learning and memory, kinases generally modulate positively while phosphatases modulate negatively. This review outlines some of the critical physiological and structural aspects of kinases and phosphatases involved in maintaining postsynaptic structural plasticity. It also explores the link between neuronal disorders and the deregulation of phosphatases and kinases. Wolters Kluwer - Medknow 2020-11-27 /pmc/articles/PMC8224123/ /pubmed/33269764 http://dx.doi.org/10.4103/1673-5374.300331 Text en Copyright: © 2021 Neural Regeneration Research https://creativecommons.org/licenses/by-nc-sa/4.0/This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms.
spellingShingle Review
Khan, Raheel
Kulasiri, Don
Samarasinghe, Sandhya
Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title_full Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title_fullStr Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title_full_unstemmed Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title_short Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
title_sort functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8224123/
https://www.ncbi.nlm.nih.gov/pubmed/33269764
http://dx.doi.org/10.4103/1673-5374.300331
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