Proteomics

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De Novo Design of Tyrosine and Serine Kinase Driven Protein Switches


ABSTRACT: : Kinases play central roles in signaling cascades, relaying information from the outside to the inside of mammalian cells1. De novo designed protein switches capable of interfacing with tyrosine kinase signaling pathways would open new avenues for controlling cellular behavior, but to date no such systems have been described. Here we describe the de novo design of two classes of protein switches which link phosphorylation by both tyrosine and serine kinases to protein-protein association. In the first class, protein-protein association drives kinase phosphorylation; addition of a designed co-regulator induces the phosphorylation of the ITAM motif central to T-cell signaling2. In the second class, kinase phosphorylation drives protein-protein association; we describe systems in which kinase action drives reconstitution of GFP fluorescence from fragments and the inhibition of the protease calpain. The designed switches are reversible and function in vitro and in cells with up to 40-fold activation of switching by phosphorylation.

INSTRUMENT(S): LTQ, Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Richard Johnson  

LAB HEAD: David Baker

PROVIDER: PXD027295 | Pride | 2022-04-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
VP_2019_0621_RJ_06_f1.raw Raw
VP_2019_0621_RJ_07_f2.raw Raw
VP_2019_0621_RJ_08_e1.raw Raw
VP_2019_0621_RJ_09_e2.raw Raw
VP_2019_0621_RJ_10_d1.raw Raw
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Publications


Kinases play central roles in signaling cascades, relaying information from the outside to the inside of mammalian cells. De novo designed protein switches capable of interfacing with tyrosine kinase signaling pathways would open new avenues for controlling cellular behavior, but, so far, no such systems have been described. Here we describe the de novo design of two classes of protein switch that link phosphorylation by tyrosine and serine kinases to protein-protein association. In the first cl  ...[more]

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