What does phosphorylation and dephosphorylation do with regards to protein activation?
What does phosphorylation and dephosphorylation do with regards to protein activation?
Phosphorylation regulates protein function and cell signaling by causing conformational changes in the phosphorylated protein. These changes can affect the protein in two ways. Thus, a protein can be either activated or inactivated by phosphorylation.
How do you interpret the significance of protein phosphorylation and dephosphorylation?
Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. Approximately 13000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases.
What does dephosphorylation do to a protein?
The dephosphorylation of proteins is a mechanism for modifying behavior of a protein, often by activating or inactivating an enzyme. Components of the protein synthesis apparatus also undergo phosphorylation and dephosphorylation and thus regulate the rates of protein synthesis.
What is the role of phosphorylation and dephosphorylation in cell signaling?
Phosphorylation and dephosphorylation are important posttranslational modifications of native proteins, occurring site specifically on a protein surface. These biological processes play important roles in intracellular signal transduction cascades and switching the enzymatic activity.
What type of enzyme is Erk?
ERK, a type of serine/threonine protein kinase, is a signal transduction protein that transmits mitogen signals (32). ERK is generally located in the cytoplasm; upon activation, ERK enters the nucleus and regulates transcription factor activity and gene expression (33).
What do you mean by dephosphorylation?
Definition of dephosphorylation : the process of removing phosphate groups from an organic compound (such as ATP) by hydrolysis also : the resulting state.
Which scaffold proteins are involved in the ERK1/2 MAP kinase cascade?
A variety of scaffold proteins including KSR1/2, IQGAP1, MP1, β-Arrestin1/2 participate in the regulation of the ERK1/2 MAP kinase cascade. The regulatory dephosphorylation of ERK1/2 is mediated by protein-tyrosine specific phosphatases, protein-serine/threonine phosphatases, and dual specificity phosphatases.
Where does memek1/2 catalyze the phosphorylation of human ERK1?
MEK1/2 catalyze the phosphorylation of human ERK1/2 at Tyr204/187 and then Thr202/185. The phosphorylation of both tyrosine and threonine is required for enzyme activation.
What is the function of ERK1 and ERK2?
ERK1 and ERK2 are related protein-serine/threonine kinases that participate in the Ras-Raf-MEK-ERK signal transduction cascade. This cascade participates in the regulation of a large variety of processes including cell adhesion, cell cycle progression, cell migration, cell survival, differentiation, …
What is the role of kinases and phosphatases in nuclear transcription?
The combination of kinases and phosphatases make the overall process reversible. The ERK1/2 catalyzed phosphorylation of nuclear transcription factors including those of Ets, Elk, and c-Fos represents an important function and requires the translocation of ERK1/2 into the nucleus by active and passive processes involving the nuclear pore.
