Details

Autor(en) / Beteiligte

• Tullis, Jonathan E
• Rumian, Nicole L
• Brown, Carolyn Nicole
• Bayer, K Ulrich
• Zha, Xiangming

Titel

The CaMKII K42M and K42R mutations are equivalent in suppressing kinase activity and targeting

Ist Teil von

• PloS one, 2020-07, Vol.15 (7), p.e0236478-e0236478

Ort / Verlag

United States: Public Library of Science

Erscheinungsjahr

2020

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• CaMKII is an important mediator of forms of synaptic plasticity that are thought to underly learning and memory. The CaMKII mutants K42M and K42R have been used interchangeably as research tools, although some reported phenotypic differences suggest that they may differ in the extent to which they impair ATP binding. Here, we directly compared the two mutations at the high ATP concentrations that exist within cells (~4 mM). We found that both mutations equally blocked GluA1 phosphorylation in vitro and GluN2B binding within cells. Both mutations also reduced but did not completely abolish CaMKII T286 autophosphorylation in vitro or CaMKII movement to excitatory synapses in neurons. Thus, despite previously suggested differences, both mutations appear to interfere with ATP binding to the same extent.