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Several signaling pathways critically involved in the embryonic development and the
modulation of gene expression are initiated from the activation of cell surface
growth factor receptors that are known receptor tyrosine kinases (RTKs).
fibroblast growth factor
receptor (FGFR)
insulin growth
factor-1 receptor
(IGF-1R)
receptor serine/threonine
kinases (TGF-βR)
receptor serine/threonine
kinases (BMPR1/2)
Upon ligand binding, these receptor kinases are fully activated and phosphorylate
downstream, intracellular kinases to initiate phosphorylation signaling cascades.
9. WWW.CREATIVE-DIAGNOSTIC.COM Importance of Protein Phosphorylation
This pervasive post-translational
modification (PTM) serves as molecular
switch mechanism, modulating diverse
protein functions including: enzymatic activity
protein turnover
conformation
localization
interactions
crosstalk with other PTMs
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we are going to talk about protein phosphorylation
Phosphorylation refers to the addition of a phosphate group (PO4) on a molecule, which is a crucial chemical reaction, especially important for protein function as this modification activates
protein Phosphorylation is the most common and important molecular mechanism of acute and reversible regulation of protein function. Through protein phosphorylation, protein function is regulated in response to extracellular stimuli both inside and outside the cell.
Due to a large number of kinases and phosphatases in the genome, the identification of the specific enzymes responsible for a given site in a given protein is immensely challenging. However, because protein kinases and phosphatases recognize local specificity determinants within proteins, it is possible to use small peptides to study the characteristics of site-specific phosphorylation.
Most proteins are found to be phosphorylated at serine, or phosphorylated at threonine residues, and many proteins involved in signal transduction are also phosphorylated at tyrosine residues.
Lots of protein kinases exhibit a strict specificity for phosphorylation of either serine/threonine or tyrosine residues.
such as insulin growth factor-1 receptor (IGF-1R), fibroblast growth factor receptor (FGFR), receptor serine/threonine kinases BMPR1/2, and receptor serine/threonine kinases TGF-βR
Induced phosphorylation activates cytoplasmic protein kinases, such as Raf, the activators of the mitogen-activated protein (MAP) kinases Erk1/2 and MEK1/2, belonging to the Ras-Raf-MEK-ERK signaling pathway, and the phosphatidylinositol 3'-kinase-activated kinase (PI3K), protein kinase B/Akt.
The phosphorylation signaling cascades also frequently regulate the translocation and activity of several transcription factors (Such as Myc and Smad1 5 8 and smad 2 3 proteins.
These signal transduction pathways are highly interactive with each other and influenced by other protein phosphatases including PTEN and PTPN11 (Shp2) that negatively control protein phosphorylation and also play critical roles in the modulation of this signaling network and the cell biology.
All those phosphorylation signaling will affect the expression of differentiation-related genes in nucleus.
Protein phosphorylation has an important role in essentially all aspects of cell biology.
Reversible protein phosphorylation is characterized by the addition of phosphate donated from ATP and the removal of phosphate from a phosphorylated protein substrate, catalyzed by protein kinase and phosphatase (PP) enzymes respectively (centre circle).
This pervasive post-translational modification (PTM) serves as molecular switch mechanism, modulating diverse protein functions including enzymatic activity, protein turnover, interactions, conformation, localization, and crosstalk with other PTMs, which in turn regulate broad cellular biological functions.
Kinases and their substrates form vast networks of dynamic protein phosphorylation within cells. These networks facilitate the transmission, processing, and storage of cellular information, allowing cells to rapidly respond to their environment.
