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Valnohova, J.

Publications and source records attributed to Valnohova, J..

2 recordsLinked to original sources

Ric8 proteins as the neomorphic partners of G alpha o in GNAO1 encephalopathies

GNAO1 mutated in pediatric encephalopathies encodes the major neuronal G-protein Go. Of >40 pathogenic mutations, most are single amino acid substitutions spreading across Go sequence. We perform extensive characterization of Go mutants showing abnormal GTP uptake and hydrolysis, and deficiencies to bind G{beta}{gamma} and RGS19. Plasma membrane localization of Go is decreased for a subset of mutations that leads to epileptic manifestations. Pathogenic mutants massively gain interaction with Ric8A/B proteins, delocalizing them from cytoplasm to Golgi. Being general G-subunit chaperones and binding multiple other proteins, Ric8A/B likely mediate the disease dominance when engaging in neomorphic interactions with pathogenic Go. As the strength of Go-Ric8B interactions correlates with disease severity, our study further identifies an efficient biomarker and predictor for clinical manifestations in GNAO1 encephalopathies. One-Sentence SummaryNeomorphic mutations in Go gain dominant interactions with Ric8A/B, correlating with severity in pediatric encephalopathies.

cell biology↗

Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo

Peripheral membrane proteins (PMPs) associate with cellular membranes through post-translational modifications like S-palmitoylation. The Golgi apparatus is generally viewed as the transitory station where palmitoyl acyltransferases (PATs) modify PMPs, which are then transported to their ultimate destinations such as the plasma membrane (PM). However, little substrate specificity among the many PATs has been determined. Here we describe the inherent partitioning of Go - -subunit of heterotrimeric Go proteins - to PM and Golgi, independent from Golgi-to-PM transport. A minimal code within Go N-terminus governs its compartmentalization and re-coding produces G protein versions with shifted localization. We establish the S-palmitoylation at the outer nuclear membrane assay ("SwissKASH") to probe substrate specificity of PATs in intact cells. With this assay, we show that PATs localizing to different membrane compartments display remarkable substrate selectivity, which is the basis for PMP compartmentalization. Our findings uncover a mechanism governing protein localization and establish the basis for innovative drug discovery.

cell biology↗