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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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,...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
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...

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Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

cGMP regulated protein kinases (cGK).

Franz Hofmann1, Dominik Bernhard, Robert Lukowski

  • 1Institut für Pharmakologie und Toxikologie der Technischen Universität, Biedersteiner Str. 29, München, 80802, Germany. hofmann@ipt.med.tu-muenchen.de

Handbook of Experimental Pharmacology
|December 18, 2008
PubMed
Summary
This summary is machine-generated.

cGMP-dependent protein kinases (cGKs) regulate smooth muscle tone, platelet aggregation, and intestinal secretion. These kinases, cGKI and cGKII, are crucial downstream effectors of NO/cGMP and ANP/cGMP signaling pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • cGMP-dependent protein kinases (cGKs) are serine/threonine kinases essential in eukaryotic signaling.
  • Two genes, prkg1 and prkg2, encode cGKI and cGKII, with prkg1 producing cGKIalpha and cGKIbeta isoforms.

Purpose of the Study:

  • To elucidate the distribution and functions of cGKI and cGKII.
  • To understand the role of cGKs as downstream effectors in NO/cGMP and ANP/cGMP pathways.

Main Methods:

  • The abstract does not specify methods, focusing on summarizing known information about cGK distribution and function.

Main Results:

  • cGKI is prevalent in smooth muscle, platelets, and specific neurons, mediating smooth muscle relaxation and inhibiting platelet aggregation.
  • cGKII is found in intestinal epithelium, juxta-glomerular cells, adrenal cortex, chondrocytes, and suprachiasmatic nucleus, inhibiting renin secretion, intestinal secretion, and bone growth.

Conclusions:

  • cGKs are critical regulators of diverse physiological processes, including smooth muscle function, platelet activity, intestinal transport, and circadian rhythms.
  • cGKs play significant roles in cell growth and various other cellular functions, highlighting their broad physiological importance.