Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Lysosomes01:31

Lysosomes

27.0K
Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
27.0K
Lysosomes01:31

Lysosomes

3.7K
3.7K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

4.7K
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
4.7K
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

5.1K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
5.1K
The Proteasome01:13

The Proteasome

2.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
2.0K
The Proteasome02:18

The Proteasome

10.5K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Autoantibody-triggered podocyte membrane budding drives autoimmune kidney disease.

Cell·2025
Same author

Call for preserving specialized knowledge and contributions of the CAT to advancing ATMPs in Europe.

Cytotherapy·2025
Same author

Leveraging the ADAM10 prodomain for selective inhibition to enhance recovery after myocardial infarction.

British journal of pharmacology·2025
Same author

Recombinant cathepsins B and L promote α-synuclein clearance and restore lysosomal function in human and murine models with α-synuclein pathology.

Molecular neurodegeneration·2025
Same author

LIMP-2 deficiency-associated glycolipid abnormalities in mice.

Biochimica et biophysica acta. Molecular and cell biology of lipids·2025
Same author

Sphingosine-1-phosphate signalling activates E-Syt1 to facilitate HDL-derived cholesterol transport.

Nature cell biology·2025

Related Experiment Video

Updated: Mar 21, 2026

Live-cell Imaging of Lysosomal Membrane Permeabilization During Necroptosis
05:30

Live-cell Imaging of Lysosomal Membrane Permeabilization During Necroptosis

Published on: November 14, 2025

537

Intramembrane proteolysis within lysosomes.

Bernd Schröder1, Paul Saftig1

  • 1Biochemisches Institut, Christian-Albrechts-Universität zu Kiel, Otto-Hahn-Platz 9, D-24118 Kiel, Germany.

Ageing Research Reviews
|May 5, 2016
PubMed
Summary

Lysosomal membrane proteolysis regulates key cellular functions, impacting immunity and neurodegeneration. This process is crucial for maintaining membrane protein homeostasis, especially in aging individuals.

Keywords:
Alzheimer DiseaseCD74Intramembrane proteolysisLysosomeSignal peptide peptidase-like 2a proteaseγ-Secretase

More Related Videos

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

3.1K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.4K

Related Experiment Videos

Last Updated: Mar 21, 2026

Live-cell Imaging of Lysosomal Membrane Permeabilization During Necroptosis
05:30

Live-cell Imaging of Lysosomal Membrane Permeabilization During Necroptosis

Published on: November 14, 2025

537
Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

3.1K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.4K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Regulated intramembrane proteolysis is vital for cellular processes.
  • Dysfunctional proteolysis is linked to neurodegeneration, cancer, and immune disorders.

Purpose of the Study:

  • To review intramembrane proteases located in the lysosomal membrane.
  • To highlight their roles in cellular function and proteostasis.

Main Methods:

  • Literature review focusing on lysosomal membrane-localized intramembrane proteases.
  • Discussion of the γ-secretase complex and signal peptide peptidase-like (SPPL) protease 2a.

Main Results:

  • γ-secretase activity in lysosomes contributes to amyloid β production and lysosomal dysfunction.
  • SPPL protease 2a cleaves substrates like CD74, FasL, and TNF, influencing immunity and neurodegeneration.

Conclusions:

  • Lysosomal membrane proteolysis regulates critical cellular functions.
  • It is essential for membrane protein homeostasis, which may decline with age.