Proteomics

Dataset Information

0

Phosphorylation of purified recombinant mouse Ric-8B


ABSTRACT: Analysis of recombinant mouse Ric-8B protein phosphorylation. Ric-8B was purified from insect cells and E.coli and both treated with protein kinase CK2 and re-purified prior to LC-MS/MS. Another Ric-8B sample from insect cells was not treated with CK2 and also subjected to LC-MS/MS.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Frank Kwarcinski  

LAB HEAD: Gregory G. Tall

PROVIDER: PXD036645 | Pride | 2024-05-23

REPOSITORIES: Pride

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Structures of Ric-8B in complex with Gα protein folding clients reveal isoform specificity mechanisms.

Papasergi-Scott Makaía M MM   Kwarcinski Frank E FE   Yu Maiya M   Panova Ouliana O   Ovrutsky Ann M AM   Skiniotis Georgios G   Tall Gregory G GG  

Structure (London, England : 1993) 20230316 5


Mammalian Ric-8 proteins act as chaperones to regulate the cellular abundance of heterotrimeric G protein α subunits. The Ric-8A isoform chaperones Gαi/o, Gα12/13, and Gαq/11 subunits, while Ric-8B acts on Gαs/olf subunits. Here, we determined cryoelectron microscopy (cryo-EM) structures of Ric-8B in complex with Gαs and Gαolf, revealing isoform differences in the relative positioning and contacts between the C-terminal α5 helix of Gα within the concave pocket formed by Ric-8 α-helical repeat el  ...[more]

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