Curated Information
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Curated Information Page
PubMed Id: 17572661 
Chan CB, et al. (2007) Akt phosphorylation of zyxin mediates its interaction with acinus-S and prevents acinus-triggered chromatin condensation. Cell Death Differ 14, 1688-99 17572661
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S142-p - Zyxin (human)
Orthologous residues
Zyxin (human): S142‑p, Zyxin (mouse): C143‑p, Zyxin (rat): S143‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of constitutively active enzyme, transfection of inactive enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 gamma (human) Induces protein stabilization co-immunoprecipitation
acinus (human) Induces protein stabilization co-immunoprecipitation
 Comments:  phosphorylation does not protect zyxin from proteolytic cleavage by caspase, but inhibits acinus degradation and suppresses apoptosis


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