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

21.4K
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,...
21.4K
Proteomics01:33

Proteomics

8.6K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
8.6K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

4.0K
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,...
4.0K
The Proteasome Structure01:17

The Proteasome Structure

1.1K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
1.1K

You might also read

Related Articles

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

Sort by
Same author

Mitochondria contact lipid droplets through the mitochondrial import complex binding to lipid metabolism enzyme Ayr1.

Nature cell biology·2026
Same author

Proteomics Insights Into Lysosome Biogenesis and Maturation.

Proteomics·2025
Same author

Lysosome Enrichment Using Superparamagnetic Iron Oxide Nanoparticles (SPIONs).

Methods in molecular biology (Clifton, N.J.)·2025
Same author

Mass Spectrometry-Based Proteomic Analysis of Lysosome-Enriched Fractions.

Methods in molecular biology (Clifton, N.J.)·2025
Same author

Nutrient-regulated control of lysosome function by signaling lipid conversion.

Cell·2025
Same author

Flotillins in membrane trafficking and physiopathology.

Biology of the cell·2025
Same journal

Elevated urea levels in human frontotemporal dementia and amyotrophic lateral sclerosis post-mortem brain tissue: Evidence of a multi-dementia pathogenic mechanism.

Molecular omics·2026
Same journal

Metabolite-centric identification of antimetabolite drug targets across cancer and neurodegenerative diseases.

Molecular omics·2026
Same journal

Platelet proteomics on less than a drop of previously frozen, non-citrate plasma.

Molecular omics·2026
Same journal

Decoding the diabetic transition: a lipidomic approach for biomarker discovery in an Indian cohort.

Molecular omics·2026
Same journal

Placental metabolomics for assessment of pregnancy complications: a systematic review.

Molecular omics·2026
Same journal

Prostate cancer: metabolic remodelling in expressed prostatic secretions reveals cellular structural changes measured by mpMRI.

Molecular omics·2026
See all related articles

Related Experiment Video

Updated: Oct 21, 2025

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

2.7K

A proteomic view on lysosomes.

Pathma Muthukottiappan1, Dominic Winter1

  • 1Institute for Biochemistry and Molecular Biology, Medical Faculty, Rheinische Friedrich-Wilhelms-University of Bonn, Nussallee 11, 53115 Bonn, Germany. dominic.winter@uni-bonn.de.

Molecular Omics
|September 3, 2021
PubMed
Summary
This summary is machine-generated.

Mass spectrometry-based proteomics has identified over 300 lysosomal proteins, crucial for cellular homeostasis and disease research. This review highlights how these methods advance our understanding of lysosomal functions and related disorders.

More Related Videos

Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome
14:23

Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome

Published on: March 7, 2014

18.9K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.4K

Related Experiment Videos

Last Updated: Oct 21, 2025

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

2.7K
Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome
14:23

Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome

Published on: March 7, 2014

18.9K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.4K

Area of Science:

  • Cell Biology
  • Biochemistry
  • Proteomics

Background:

  • Lysosomes are vital eukaryotic organelles responsible for cellular degradation and homeostasis.
  • Lysosomal dysfunction is linked to numerous diseases, and lysosomes are increasingly recognized as regulators of cellular metabolism and signaling.
  • Over 300 proteins have been identified in or at lysosomes, with ongoing research expanding the known lysosomal proteome and interactome.

Purpose of the Study:

  • To review the application of mass spectrometry (MS)-based proteomics in investigating the lysosomal proteome.
  • To summarize how MS-based approaches have been used to address diverse research questions concerning lysosomes.
  • To highlight the role of proteomics in understanding lysosome-related disorders and identifying disease biomarkers.

Main Methods:

  • Utilizing mass spectrometry (MS)-based proteomics for the identification and characterization of lysosomal proteins.
  • Employing various enrichment strategies for lysosomes or lysosomal proteins prior to MS analysis.
  • Analyzing data from >60 studies across different model organisms and pathological conditions.

Main Results:

  • MS-based proteomics has successfully characterized the lysosomal proteome and its associated interactome.
  • These methods have facilitated the investigation of lysosome-related disorders and the identification of lysosomal proteins as potential disease biomarkers.
  • Proteomics has aided in elucidating lysosome-associated cellular mechanisms and signaling pathways.

Conclusions:

  • Mass spectrometry-based proteomics is an indispensable tool for studying the lysosomal proteome and its role in cellular function and disease.
  • Despite significant progress, many proteomics approaches remain to be applied to lysosome research, indicating substantial opportunities for future investigations.
  • Continued application of advanced proteomics techniques will further unravel the complexities of lysosomal biology and its implications for human health.