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

Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

You might also read

Related Articles

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

Sort by
Same author

K48-ubiquitin-dependent proteases cut-up post-ER proteins.

Nature communications·2026
Same author

Insulated piggyBac and FRT vectors for engineering transgenic homozygous and heterozygous eHAP cells.

Biology open·2025
Same author

Charcot-Marie-Tooth disease type 1E: clinical natural history and molecular impact of PMP22 variants.

Brain : a journal of neurology·2025
Same author

Charcot-Marie-Tooth disease type 1E: Clinical Natural History and Molecular Impact of <i>PMP22</i> Variants.

medRxiv : the preprint server for health sciences·2025
Same author

Disrupting the transmembrane domain interface between PMP22 and MPZ causes peripheral neuropathy.

iScience·2025
Same author

Loss of HD-PTP function results in lipodystrophy, defective cellular signaling and altered lipid homeostasis.

Journal of cell science·2024

Related Experiment Video

Updated: Jul 14, 2026

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
09:01

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Biogenesis and function of multivesicular bodies.

Robert C Piper1, David J Katzmann

  • 1Department of Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA. robert-piper@uiowa.edu

Annual Review of Cell and Developmental Biology
|May 18, 2007
PubMed
Summary

Ubiquitin tagging guides membrane proteins to cellular degradation sites. Recent discoveries highlight proteins involved in multivesicular body formation, but their precise molecular functions in protein sorting remain unclear.

More Related Videos

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Construction of Out&#45;of&#45;Equilibrium Metabolic Networks in Nano&#45; and Micrometer&#45;Sized Vesicles
10:56

Construction of Out-of-Equilibrium Metabolic Networks in Nano- and Micrometer-Sized Vesicles

Published on: April 12, 2024

Related Experiment Videos

Last Updated: Jul 14, 2026

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
09:01

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Construction of Out&#45;of&#45;Equilibrium Metabolic Networks in Nano&#45; and Micrometer&#45;Sized Vesicles
10:56

Construction of Out-of-Equilibrium Metabolic Networks in Nano- and Micrometer-Sized Vesicles

Published on: April 12, 2024

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Degradation

Background:

  • Membrane proteins are degraded via the proteasome or lysosome.
  • Ubiquitin attachment acts as a crucial sorting signal for both degradation pathways.
  • Lysosomal degradation involves sorting ubiquitinated proteins into multivesicular bodies (MVBs) for subsequent lysosomal degradation.

Purpose of the Study:

  • To review recent advancements in understanding the molecular mechanisms of multivesicular body (MVB) biogenesis and function.
  • To identify key proteins involved in the sorting and degradation of membrane proteins via the lysosomal pathway.
  • To highlight outstanding questions regarding the precise roles of these proteins in MVB formation and cargo trafficking.

Main Methods:

  • Literature review of recent research (past five years) on MVB biogenesis and protein degradation.
  • Analysis of studies identifying proteins involved in ubiquitination, cargo sorting, and vesicle formation.
  • Synthesis of current knowledge on the lysosomal degradation pathway for membrane proteins.

Main Results:

  • Ubiquitination is essential for targeting proteins to the MVB lumen.
  • MVB formation involves endosomal membrane invagination and intralumenal vesicle budding.
  • Several new proteins have been implicated in MVB biogenesis and cargo sorting.
  • The precise molecular functions of these newly identified proteins are largely unknown.

Conclusions:

  • The lysosomal degradation pathway, particularly MVB formation, is a complex process reliant on specific ubiquitination and protein sorting machinery.
  • Recent discoveries have expanded the known protein players in MVB biogenesis.
  • Further research is needed to elucidate the molecular mechanisms by which these proteins mediate cargo selection, sorting, and intralumenal vesicle formation.