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Oguz Can Koc

As seen in: ACS Publications, BioRxiv
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Articles

Phosphoproteomic Analysis of Cortical Tissue from Mice Lacking Both CaMKIIα and CaMKIIβ Identifies Novel In Vivo Substrates

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By Karel Bezstarosti, Oguz Can Koc, Pomme M. F. Rigter
| ACS Publications
Cite Jump to ExpandCollapse Research ArticleFebruary 25, 2026 Phosphoproteomic Analysis of Cortical Tissue from Mice Lacking Both CaMKIIα and CaMKIIβ Identifies Novel In Vivo Substrates Click to copy article linkArticle link copied! Pomme M. F. Rigter Pomme M. F.
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A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation

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By Can Ozden, Kairong Dong, Oguz Can Koc, Ana Pamela Torres-Ocampo
| BioRxiv
Abstract Memory formation, fertilization, and cardiac function rely on precise Ca2+ signaling and subsequent Ca2+/calmodulin-dependent protein kinase II (CaMKII) activation. Ca2+ sensitivity of the four CaMKII paralogs in mammals has been linked to the length of the variable linker region that is a hot spot for alternative splicing. In this study, we determined that the position of charged residues within the linker modulates the Ca2+/CaM sensitivity.
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Simultaneous loss of CAMK2A and CAMK2B reveals endogenous in vivo substrates

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By Karel Bezstarosti, Tyler L Perfitt, Pomme M.F. Rigter, Oguz Can Koc
| BioRxiv
Abstract Ca2+/calmodulin-dependent protein kinase 2 (CAMK2) plays a critical role in calcium signaling. Recent gene knockout studies show that CAMK2A and CAMK2B can have distinct roles yet also partially compensate for each other in yet unknown brain functions.
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