1932

Abstract

Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein kinases and protein phosphatases that modulate the phosphorylation status of proteins. This review discusses recent advances in our understanding of the structure, regulation, and function of plant protein phosphatases. Three major classes of enzymes have been reported in plants that are homologues of the mammalian type-1, -2A, and -2C protein serine/threonine phosphatases. Molecular genetic and biochemical studies reveal a role for some of these enzymes in signal transduction, cell cycle progression, and hormonal regulation. Studies also point to the presence of additional phosphatases in plants that are unrelated to these major classes.

Loading

Article metrics loading...

/content/journals/10.1146/annurev.arplant.47.1.101
1996-06-01
2024-04-25
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.arplant.47.1.101
Loading
/content/journals/10.1146/annurev.arplant.47.1.101
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error