Time to Search for Protein Kinase Substrates

2008 ◽  
pp. 485-498 ◽  
Author(s):  
Birgit Kersten
Keyword(s):  
Protein Kinase ◽  
Kinase Substrates

Identification of protein kinase substrates by proteomic approaches

2008 ◽  
Vol 5 (3) ◽  
pp. 497-505 ◽  
Author(s):  
Seisuke Hattori ◽  
Naoyuki Iida ◽  
Hidetaka Kosako
Keyword(s):  
Protein Kinase ◽  
Kinase Substrates

scholarly journals Combining chemical genetics and proteomics to identify protein kinase substrates

2005 ◽  
Vol 102 (50) ◽  
pp. 17940-17945 ◽  
Author(s):  
N. Dephoure ◽  
R. W. Howson ◽  
J. D. Blethrow ◽  
K. M. Shokat ◽  
E. K. O'Shea
Keyword(s):  
Protein Kinase ◽  
Chemical Genetics ◽  
Kinase Substrates

scholarly journals Phosphorylation-dependent substrate selectivity of protein kinase B (AKT1)

2020 ◽  
Vol 295 (24) ◽  
pp. 8120-8134
Author(s):  
Nileeka Balasuriya ◽  
Norman E. Davey ◽  
Jared L. Johnson ◽  
Huadong Liu ◽  
Kyle K. Biggar ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase B ◽  
Tumor Biology ◽  
Peptide Libraries ◽  
Substrate Selectivity ◽  
Activity Data ◽  
Cellular Processes ◽  
Substrate Preferences ◽  
Substrate Peptide ◽  
Kinase Substrates

Protein kinase B (AKT1) is a central node in a signaling pathway that regulates cell survival. The diverse pathways regulated by AKT1 are communicated in the cell via the phosphorylation of perhaps more than 100 cellular substrates. AKT1 is itself activated by phosphorylation at Thr-308 and Ser-473. Despite the fact that these phosphorylation sites are biomarkers for cancers and tumor biology, their individual roles in shaping AKT1 substrate selectivity are unknown. We recently developed a method to produce AKT1 with programmed phosphorylation at either or both of its key regulatory sites. Here, we used both defined and randomized peptide libraries to map the substrate selectivity of site-specific, singly and doubly phosphorylated AKT1 variants. To globally quantitate AKT1 substrate preferences, we synthesized three AKT1 substrate peptide libraries: one based on 84 “known” substrates and two independent and larger oriented peptide array libraries (OPALs) of ∼1011 peptides each. We found that each phospho-form of AKT1 has common and distinct substrate requirements. Compared with pAKT1T308, the addition of Ser-473 phosphorylation increased AKT1 activities on some, but not all of its substrates. This is the first report that Ser-473 phosphorylation can positively or negatively regulate kinase activity in a substrate-dependent fashion. Bioinformatics analysis indicated that the OPAL-activity data effectively discriminate known AKT1 substrates from closely related kinase substrates. Our results also enabled predictions of novel AKT1 substrates that suggest new and expanded roles for AKT1 signaling in regulating cellular processes.

Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates

Nature ◽  
1992 ◽  
Vol 356 (6364) ◽  
pp. 68-71 ◽  
Author(s):  
Xosé R. Bustelo ◽  
Jeffrey A. Ledbetter ◽  
Mariano Barbacid
Keyword(s):  
Protein Kinase ◽  
New Class ◽  
Tyrosine Protein Kinase ◽  
Kinase Substrates

Aza-β3-amino acid containing peptidomimetics as cAMP-dependent protein kinase substrates

2010 ◽  
Vol 38 (5) ◽  
pp. 229-233 ◽  
Author(s):  
Ksenija Kisseljova ◽  
Aleksei Kuznetsov ◽  
Michèle Baudy-Floc’h ◽  
Jaak Järv
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase Substrates
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