Margaret Stratton, Associate Professor of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA, will give a talk titled, "Tuning a Master Kinase: How CaMKII variants are deployed and degraded."

This seminar will also be available by Zoom. Zoom link:  https://gc-cuny.zoom.us/j/99611592897?pwd=gB1rITJuytSxEjCZIKEhpdaepER3u…

Meeting ID:  996 1159 2897     Passcode:  asrc+CCNY

Please note: 

* Full names must be used to be admitted to the Zoom meeting.

* The Zoom meeting will be closed and locked at 12:15 p.m., and no one will be able to enter the meeting after that time.

ABSTRACT

Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) is a central signaling enzyme that regulates neuronal plasticity, fertilization, and cardiac function. Although its catalytic and oligomerization domains are highly conserved, extensive alternative splicing within a variable linker region generates numerous CaMKII proteoforms whose functional roles remain unclear. Transcript sequencing of human hippocampus reveals three CaMKIIα splice variants in human hippocampal tissue. Biochemical and cellular analyses show that linker composition tunes CaMKII activation by Ca²⁺/calmodulin, with electrostatic effects that modulate regulatory segment accessibility. In addition to activation control, CaMKII signaling is regulated by selective degradation: activated CaMKII is targeted by the ubiquitin–proteasome system. Together, these results reveal how alternative splicing and ubiquitin-dependent turnover cooperate to tune the activity of this master kinase.