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Related Concept Videos

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,...
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PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Actin Polymerization01:42

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
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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

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Related Experiment Video

Updated: Jun 24, 2026

Live-imaging of PKC Translocation in Sf9 Cells and in Aplysia Sensory Neurons
09:54

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Published on: April 6, 2011

Skp2: caught in the Akt.

Karin Ecker, Ludger Hengst

    Nature Cell Biology
    |April 2, 2009
    PubMed
    Summary
    This summary is machine-generated.

    The Akt kinase phosphorylates Skp2, a key component of the SCF-Skp2 ubiquitin ligase. This action activates the SCF-Skp2 complex, which regulates cell-cycle progression.

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    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Signal Transduction

    Background:

    • Cell proliferation is tightly controlled by signal transduction pathways regulating the cell cycle.
    • The SCF-Skp2 ubiquitin ligase complex targets key regulators of the cell cycle for degradation.

    Discussion:

    • Akt, a central kinase in diverse signaling networks, phosphorylates Skp2.
    • Skp2 is a crucial subunit of the SCF-Skp2 ubiquitin ligase.
    • Akt1-dependent phosphorylation activates the SCF-Skp2 complex through various mechanisms.

    Key Insights:

    • Akt directly regulates the SCF-Skp2 ubiquitin ligase activity via Skp2 phosphorylation.
    • This phosphorylation event is a critical step in controlling cell-cycle progression.
    • The findings elucidate a novel mechanism of Akt-mediated regulation of cell division.

    Outlook:

    • Further investigation into the specific mechanisms of SCF-Skp2 activation by Akt.
    • Exploring the therapeutic potential of targeting the Akt-Skp2 interaction in cell proliferation disorders.
    • Understanding the broader implications of this regulatory axis in cancer biology.