New concept for uncoupling receptor-receptor interactions | 48054

Journal of Neurology & Neurophysiology

ISSN - 2155-9562

New concept for uncoupling receptor-receptor interactions

2nd International Conference and Exhibition on Neurology & Therapeutics

June 17-19, 2013 Hilton Chicago/Northbrook, Chicago, USA

Amina S. Woods

Scientific Tracks Abstracts: J Neurol Neurophysiol

Abstract :

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 recognition 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 [ Neuroscience . 238, 335-344 (2013)]

Biography :

Amina Sarah Woods working as a Tenure-track scientist, Head of the structural biology Unit at the Intramural Research Program (IRP), National Institute on Drug Abuse (NIDA). She manage as a Member of the editorial board of the Journal of the American Society for Mass spectrometry (2007- 2012). She chaired major sessions in major International Conferences. She have more than 160 publications in Peer Reviewed Journals. She is having prominent publications in various book chapters. She Reviews scientific papers for the major journals.