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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Cell Specific Gene Expression01:58

Cell Specific Gene Expression

Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Positive Regulator Molecules02:39

Positive Regulator Molecules

Mitotic cell division results in daughter cells that exactly resemble the parent cell. However, errors in the DNA replication or distribution of genetic material may lead to genetic mutations that may be passed down to every new cell formed from the resulting abnormal cell. Propagation of such mutant cells is restricted through checkpoint mechanisms present at different stages of the cell cycle. These checkpoints involve regulator molecules that either promote or demote cell cycle events.

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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

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Published on: August 29, 2015

Protein kinases, from B to C.

A J Cameron1, M De Rycker, V Calleja

  • 1Protein Phosphorylation Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.

Biochemical Society Transactions
|October 25, 2007
PubMed
Summary
This summary is machine-generated.

Protein kinase B (PKB) and protein kinase C (PKC) have similar catalytic domains but distinct phosphorylation dynamics. Their regulatory domains

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein kinase B (PKB) and protein kinase C (PKC) share homologous catalytic domains.
  • Optimal activity for both kinase families relies on conserved phosphorylation events.
  • Despite structural similarities, their in-cell modification dynamics differ significantly.

Purpose of the Study:

  • To investigate the mechanisms behind the distinct phosphorylation dynamics of PKB and PKC.
  • To explore the role of regulatory domains in modulating catalytic activity.
  • To understand the fundamental differences in PKB and PKC protein behavior.

Main Methods:

  • Experimental analysis of phosphorylation dynamics.
  • Comparative study of regulatory and catalytic domain interactions.
  • Biophysical characterization of protein ground states.

Main Results:

  • PKB and PKC exhibit divergent phosphorylation dynamics in cellular environments.
  • Regulatory domain interactions with catalytic domains are key determinants of these differences.
  • Distinct protein ground states underlie the unique behaviors of PKB and PKC.

Conclusions:

  • The variant regulatory domains of PKB and PKC interact distinctively with their catalytic counterparts.
  • These differential interactions dictate the unique phosphorylation dynamics observed in cells.
  • The inherent ground states of PKB and PKC proteins define their divergent functional behaviors.