NIH Proteomics Interest Group

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ProtIG is an NIH Special Interest Group (SIG) that organizes seminars and workshops in relevant areas of proteomics, including talks on separation and protein identification methods, determination of post-translational modifications, protein-protein interactions, and bioinformatics and data management. A monthly seminar series is usually held at 9:30am on the first Thursday of each month (always check the Mtgs/Seminars button on this page for these and other PROTIG announced meetings). To receive email announcements of ProtIG events, join the listserv (Join the SIG button on this page)

Extra February ProtIG Seminar
February 23rd, 2017
9:30am - 10:30am
Building 50, NIH Campus
Room 1328/1334
Amina S. Woods, Ph.D.
Chief, Structural Biology Unit, Integrative Neuroscience,
National Institute on Drug Abuse, National Institutes of Health
Adjunct Professor of Pharmacology and Molecular Sciences
Johns Hopkins School of Medicine


"The Role of Phosphorylation in G Protein coupled Receptors heteromerization."

Our work suggests that heteromer formation, mainly involves linear motifs found in disordered regions of proteins. Local disorder imparts plasticity to linear motifs. Many molecular recognitions of proteins occur between short linear segments, known as LMs. Interaction of short continuous epitopes are not constrained by sequence and have the advantage of resulting in interactions with micromolar affinities which suites transient, reversible complexes such as receptor heteromers. Electrostatic Interactions between epitopes of the GPCR involved, is the Key step in driving heteromer formation forward. The first step in heteromerization, involves phosphorylating the Ser/Thr in an epitope containing a casein kinase 1/2 (CK1/2)-consensus site. Our data suggests that dopaminergic neurotransmission, through cAMP dependent PKA slows down heteromerization. The negative charge, acquired by the phosphorylation of a Ser/Thr in a PKA consensus site in the Arg rich epitope, affects the activity of the receptors involved in heteromerization by causing allosteric conformational changes, due to the repulsive effect generated by the negatively charged phosphate. In addition to modulating heteromerization, it affects the stability of the heteromers ’interactions and their binding affinity. So here we have an instance where phosphorylation is not just an on/off switch, instead by weakening the noncovalent bond, heteromerization acts like a rheostat that controls the stability of the heteromer through activation or inhibition of adenylate cyclase by the neurotransmitter Dopamine depending on which Dopamine receptor it docks at.



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This site was updated on February 16th, 2017. Please contact Renee Olano at olanol(at)mail.nih.gov with questions or suggestions.