Abstract
Beta arrestins are molecular scaffolds that can bring together three-component mitogen-activated protein kinase signalling modules to promote signal compartmentalisation. We use peptide array technology to define novel interfaces between components within the c-Jun N-terminal kinase (JNK)/beta arrestin signalling complex. We show that beta arrestin 1 and beta arrestin 2 associate with JNK3 via the kinase N-terminal domain in a region that, surprisingly, does not harbour a known 'common docking' motif. In the N-domain and C-terminus of beta arrestin 1 and beta arrestin 2 we identify two novel apoptosis signal-regulating kinase 1 binding sites and in the N-domain of the beta arrestin 1 and beta arrestin 2 we identify a novel MKK4 docking site.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Arrestins / chemistry*
-
Arrestins / genetics
-
Arrestins / metabolism*
-
MAP Kinase Kinase 4 / chemistry
-
MAP Kinase Kinase 4 / genetics
-
MAP Kinase Kinase 4 / metabolism
-
MAP Kinase Signaling System / physiology*
-
Mitogen-Activated Protein Kinase 10 / chemistry*
-
Mitogen-Activated Protein Kinase 10 / genetics
-
Mitogen-Activated Protein Kinase 10 / metabolism*
-
Models, Molecular
-
Molecular Sequence Data
-
Peptide Library
-
Peptides / genetics
-
Peptides / metabolism*
-
Protein Array Analysis / methods*
-
Protein Binding
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
-
beta-Arrestins
Substances
-
Arrestins
-
Peptide Library
-
Peptides
-
Recombinant Fusion Proteins
-
beta-Arrestins
-
Mitogen-Activated Protein Kinase 10
-
MAP Kinase Kinase 4