Mechanisms for localising calcineurin and CaMKII in dendritic spines

Cellular Signalling
Christopher J Penny, Matthew G Gold

Abstract

Calcineurin and calmodulin-dependent protein kinase II (CaMKII) are both highly abundant in neurons, and both are activated by calmodulin at similar Ca2+ concentrations in the test tube. However, they fulfill opposite functions in dendritic spines, with CaMKII activity driving long-term synaptic potentiation following large influxes of Ca2+ through NMDA-type glutamate receptors (NMDARs), and calcineurin responding to smaller influxes of Ca2+ through the same receptors to induce long-term depression. In this review, we explore the notion that precise dynamic localisation of the two enzymes at different sites within dendritic spines is fundamental to this behaviour. We describe the structural basis of calcineurin and CaMKII localisation by their interaction with proteins including AKAP79, densin-180, α-actinin, and NMDARs. We then consider how interactions with these proteins likely position calcineurin and CaMKII at different distances from Ca2+ microdomains emanating from the mouths of NMDARs in order to drive the divergent responses. We also highlight shortcomings in our current understanding of synaptic localisation of these two important signalling enzymes.

Citations

Oct 17, 2018·PloS One·Ayse DosemeciThomas S Reese
Nov 30, 2018·The Journal of Physiology·Moriah GildartKimberly L Dodge-Kafka
Jan 5, 2019·Biological Reviews of the Cambridge Philosophical Society·Alessandra DonatoMassimo A Hilliard
Sep 20, 2019·Neural Regeneration Research·Bor Luen Tang
Nov 28, 2019·Biological Reviews of the Cambridge Philosophical Society·Danton H O'DayRobert J Huber
Nov 19, 2019·Frontiers in Synaptic Neuroscience·Amita ShresthaOlalekan M Ogundele
Jul 1, 2020·Proceedings of the National Academy of Sciences of the United States of America·Ga-Yeon SonIndu Suresh Ambudkar
Sep 19, 2020·Scientific Reports·Kazuya KuboyamaMaki K Yamada

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