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Related Concept Videos

Autophagy01:27

Autophagy

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Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
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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...
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Autophagic Cell Death01:18

Autophagic Cell Death

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Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
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Delivery Pathways to the Lysosome01:36

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
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Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

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Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...
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The JAK-STAT Signaling Pathway01:20

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Related Experiment Video

Updated: May 5, 2026

Study of Protein-protein Interactions in Autophagy Research
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DAP-kinase and autophagy.

Vered Levin-Salomon1, Shani Bialik, Adi Kimchi

  • 1Department of Molecular Genetics, Weizmann Institute of Science, 76100, Rehovot, Israel.

Apoptosis : an International Journal on Programmed Cell Death
|November 23, 2013
PubMed
Summary

Death-associated protein kinase (DAPK) promotes autophagy initiation by regulating the Vps34 complex through two distinct pathways. These findings link DAPK

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Death-associated protein kinase (DAPK) is a Ca(2+)-calmodulin regulated kinase involved in apoptosis, cytoskeletal dynamics, and immune functions.
  • DAPK has recently emerged as a key regulator of autophagy, a cellular process for degrading cytoplasmic components via autophagosomes.

Purpose of the Study:

  • To elucidate the mechanisms by which DAPK modulates the induction stage of autophagy.
  • To explore additional DAPK-autophagy connections and their implications in disease.

Main Methods:

  • Investigated DAPK's role in Vps34 class III phosphatidyl inositol 3-kinase complex regulation.
  • Analyzed kinase cascades involving DAPK, protein kinase D, and Vps34.
  • Examined direct phosphorylation of Beclin 1 by DAPK and its interaction with Bcl-2.

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Main Results:

  • DAPK positively regulates autophagosome nucleation through two mechanisms involving the Vps34 complex.
  • Mechanism 1: DAPK phosphorylates protein kinase D, which activates Vps34.
  • Mechanism 2: DAPK directly phosphorylates Beclin 1, releasing it from Bcl-2 inhibition.

Conclusions:

  • DAPK plays a crucial role in initiating autophagy via modulation of the Vps34 complex.
  • Further research is needed to fully validate DAPK's involvement in other autophagy-related processes.
  • DAPK's role in autophagy may connect to its tumor suppressor functions and implications in neurodegenerative diseases.