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Phosphorylation and prolyl isomerization independently regulate the signal adapter function of CrkII.

Title data

Schmidpeter, Philipp A. M. ; Schmid, Franz X.:
Phosphorylation and prolyl isomerization independently regulate the signal adapter function of CrkII.
In: Journal of Molecular Biology. Vol. 426 (12 December 2014) Issue 24 . - pp. 3929-3934.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2014.09.022

Abstract in another language

The signaling protein CrkII switches between forms with high or low binding affinity. Both phosphorylation and native-state prolyl isomerization were suggested to regulate the transition between these forms. Here we analyzed how phosphorylation at Tyr222 and Tyr252 and the Pro238Ala substitution affect signal transfer of human and chicken CrkII to a downstream target. Human CrkII is regulated by phosphorylation only, but chicken CrkII is regulated by Pro238 trans→cis isomerization and by Tyr222 phosphorylation. Surprisingly, they act in an independent fashion. Apparently, the allosteric transition to a low-activity form can be induced by phosphorylation or prolyl isomerization located at distant sites in CrkII.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 25284755
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 21 Apr 2015 13:14
Last Modified: 10 Jun 2015 14:27
URI: https://eref.uni-bayreuth.de/id/eprint/10470