Sandra Berndt
Post-doctoral fellow, Pharmacology
Sandra joined the lab in June 2015, left in 2019 to take a position in Leipzig University, Germany.
Sandra got her Masters (2009) and PhD (magna cum laude; 2014) degrees from University of Leipzig (Advisor: Prof. Daniel Huster), Germany.
In 2013-15 Sandra worked as a postdoc at Cambridge University (UK), in the Department of Biochemistry (advisor: Dr. Daniel Nietlispach)
Research Description
Sandra is working on structure-function studies of arrestin-1 and arrestin-3.
To get an insight into the molecular mechanism of arrestin-1 binding to its cognate receptor, rhodopsin, Sandra is introducing single cysteines into cys-less base mutant to measure distances between selected positions of arrestin-1 and rhodopsin. This info will help us elucidate the structure of different “flavors” of the complex, that form depending on rhodopsin phosphorylation level and possibly the positions of the phosphates in rhodopsin.
Sandra is also generating mutants to test our recent crystal structure of active arrestin-3 conformation (solved by Qiuyan Chen and Tina Iverson). She is introducing pairs of cysteines to “lock” the protein in the basal or active state. These mutants will be used to test the effect of generated conformational bias on receptor binding and JNK3 activation.
Sandra is also working on crystallization of arrestin-3 elements that bind JNK3 with this kinase.
Papers from the lab
Chen, Q., Zhuo, Y., Sharma, P., Perez, I., Francis, D.J., Chakravarthy, S., Vishnivetskiy, S.A., Berndt, S., Hanson, S.M., Zhan, X., Brooks, E.K., Altenbach, C., Hubbell, W.L., Klug, C.S., Iverson, T.M., Gurevich, V.V. An eight amino acid segment controls oligomerization and preferred conformation of the two non-visual arrestins. J Mol Biol 433 (4), 166790; doi: 10.1016/j.jmb.2020.166790 (2021).
Berndt, S., Gurevich, V.V., Iverson, T.M. Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase. PLoS One, in press (2019).
Perry, N.A., Kaoud, T.S., Ortega, O.O., Kaya, A.I., Marcus, D.J., Pleinis, J.M., Berndt, S., Chen, Q., Zhan, X., Dalby, K.N., Lopez, C.F., Iverson, T.M., Gurevich, V.V. Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification. Proc Natl Acad Sci USA 116 (3), 810-815; doi: 10.1073/pnas.1819230116 (2019).
Chen, Q., Perry, N.A., Vishnivetskiy, S.A., Berndt, S., Gilbert, N.C., Zhuo, Y., Singh, P.K., Tholen, J., Ohi, M.D., Gurevich, E.V., Brautigam, C.A., Klug, C.S., Gurevich, V.V., Iverson, T.M. Structural basis of arrestin-3 activation and signaling. Nat Commun 8, 1427; doi: 10.1038/s41467-01701218-8 (2017).
Berndt, S., Gurevich, V.V., Gurevich, E.V. Arrestins in cell death. Ch 19 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).