Molecular basis for cellular retinoic acid-binding protein 1 in modulating CaMKII activation.

ABSTRACT: Introduction: Cellular retinoic acid (RA)-binding protein 1 (CRABP1) is a highly conserved protein comprised of an anti-parallel, beta-barrel, and a helix-turn-helix segment outside this barrel. Functionally, CRABP1 is thought to bind and sequester cytosolic RA. Recently, CRABP1 has been established as a major mediator of rapid, non-genomic activity of RA in the cytosol, referred to as "non-canonical" activity. Previously, we have reported that CRABP1 interacts with and dampens the activation of calcium-calmodulin (Ca²⁺-CaM)-dependent kinase 2 (CaMKII), a major effector of Ca²⁺ signaling. Through biophysical, molecular, and cellular assays, we, herein, elucidate the molecular and structural mechanisms underlying the action of CRABP1 in dampening CaMKII activati

SUBMITTER: Nhieu J 

PROVIDER: S-EPMC10562560 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature