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TitleIt takes two transducins to activate the cGMP-phosphodiesterase 6 in retinal rods.
Journal, issue, pagesOpen Biol, Vol. 8, Issue 8, Year 2018
Publish dateMar 22, 2019
AuthorsBilal M Qureshi / Elmar Behrmann / Johannes Schöneberg / Justus Loerke / Jörg Bürger / Thorsten Mielke / Jan Giesebrecht / Frank Noé / Trevor D Lamb / Klaus Peter Hofmann / Christian M T Spahn / Martin Heck /
PubMed AbstractAmong cyclic nucleotide phosphodiesterases (PDEs), PDE6 is unique in serving as an effector enzyme in G protein-coupled signal transduction. In retinal rods and cones, PDE6 is membrane-bound and ...Among cyclic nucleotide phosphodiesterases (PDEs), PDE6 is unique in serving as an effector enzyme in G protein-coupled signal transduction. In retinal rods and cones, PDE6 is membrane-bound and activated to hydrolyse its substrate, cGMP, by binding of two active G protein α-subunits (Gα*). To investigate the activation mechanism of mammalian rod PDE6, we have collected functional and structural data, and analysed them by reaction-diffusion simulations. Gα* titration of membrane-bound PDE6 reveals a strong functional asymmetry of the enzyme with respect to the affinity of Gα* for its two binding sites on membrane-bound PDE6 and the enzymatic activity of the intermediary 1 : 1 Gα* · PDE6 complex. Employing cGMP and its 8-bromo analogue as substrates, we find that Gα* · PDE6 forms with high affinity but has virtually no cGMP hydrolytic activity. To fully activate PDE6, it takes a second copy of Gα* which binds with lower affinity, forming Gα* · PDE6 · Gα*. Reaction-diffusion simulations show that the functional asymmetry of membrane-bound PDE6 constitutes a coincidence switch and explains the lack of G protein-related noise in visual signal transduction. The high local concentration of Gα* generated by a light-activated rhodopsin molecule efficiently activates PDE6, whereas the low density of spontaneously activated Gα* fails to activate the effector enzyme.
External linksOpen Biol / PubMed:30068566 / PubMed Central
MethodsEM (single particle)
Resolution28.0 Å
Structure data

EMDB-0102:
symmetric structure of tPDE6
Method: EM (single particle) / Resolution: 28.0 Å

Source
  • Bos taurus (cattle)

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