Humboldt-Universität zu Berlin - Experimentelle Biophysik

Dr. Carlos Gasser


Carlos Büro


Room:  404


Tel:     (030) 2093 98276

The second messengers 3',5'-cyclic adenosine monophosphate (cAMP) and cyclic 3',5'-cyclic guanosine monophosphate (cGMP) mediate various biological responses like apoptosis, smooth muscle relaxation and vision. Cyclic-nucleotide-dependent processes have been analyzed with spatiotemporal resolution through optogenetics. In particular, genetically encoded light-activated nucleotidyl cyclases have been employed to synthesize cAMP and cGMP in living cells and organisms. For example, the fungal rhodopsin-guanylyl cyclase RhGC was shown to induce light-dependent cGMP signaling in neurons (Scheib et al., Sci Signal, 8, 2015). The complementary light-controlled breaking of cAMP and cGMP has been achieved through the synthetic light-activated phosphodiesterase (LAPD) in zebra fish embryos (Gasser et al., PNAS, 111, 2014). The aim of my project is the isolation and characterization of a natural phosphodiesterase (PDE), that catalyzes the degradation of cyclic nucleotides in a light-dependent manner. Microbial genome and transcriptome mining lead to the emergence of photoreceptor-coupled phosphodiesterase candidates. A functional light-activated PDE could allow optogenetic analysis of diverse cGMP/cAMP-mediated and membrane located processes in cells and vertebrate model organisms.



C.H. Schumacher, H.G. Körschen, C. Nicol, C. Gasser, R. Seifert, M. Schwärzel, A. Möglich, A fluorometric activity assay for light-regulated cyclic-nucleotide-monophosphate actuators, Optogenetics – Methods Mol Biol, 1408 (2016) 93–105.


C. Gasser, S. Taiber, C.-M. Yeh, C.H. Wittig, P. Hegemann, S. Ryu, F. Wunder, A. Möglich, Engineering of a red-light-activated human cAMP/cGMP-specific phosphodiesterase, PNAS, 111 (2014) 8803–8808.