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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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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.
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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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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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Study of Protein-protein Interactions in Autophagy Research
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Study of Protein-protein Interactions in Autophagy Research

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Chaperone-Mediated Autophagy.

Qian Yang1, Ronglin Wang2, Lin Zhu2

  • 1Department of Neurosurgery, Tangdu Hospital, The Fourth Military Medical University, Xi'an, China. qianyang@fmmu.edu.cn.

Advances in Experimental Medicine and Biology
|November 29, 2019
PubMed
Summary
This summary is machine-generated.

Chaperone-mediated autophagy (CMA) degrades proteins to maintain cell health. Dysfunctional CMA, due to aging or oxidative stress, contributes to diseases like cancer and neurodegeneration.

Keywords:
Basic processChaperone-mediated autophagy (CMA)MicroautophagyPhysiological functionRegulation

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein homeostasis is crucial for cell survival, regulated by synthesis and degradation.
  • Chaperone-mediated autophagy (CMA) is a key lysosomal pathway for selective protein degradation.
  • CMA dysfunction is implicated in various pathologies, including neurodegenerative diseases and cancer.

Purpose of the Study:

  • To summarize the fundamental processes of CMA.
  • To elucidate the regulatory mechanisms governing CMA.
  • To discuss the physiological roles and disease relevance of CMA.

Main Methods:

  • Literature review and synthesis of current research findings.
  • Analysis of molecular mechanisms underlying CMA substrate recognition, unfolding, and translocation.
  • Examination of CMA's role in cellular activities and disease pathogenesis.

Main Results:

  • CMA involves substrate recognition, unfolding, translocation, and lysosomal degradation.
  • CMA activity is influenced by factors like peroxide accumulation and aging.
  • Impaired CMA function is linked to the development of significant human diseases.

Conclusions:

  • CMA is a vital cellular process for maintaining protein homeostasis.
  • Understanding CMA regulation and function is critical for addressing CMA-related diseases.
  • Targeting CMA may offer therapeutic strategies for neurodegenerative diseases and cancer.