Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Overview of Secretory Vesicles

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...

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

Clathrin Coated Vesicles

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...

Receptor Downregulation in MVBs

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...

Intralumenal Vesicles and Multivesicular Bodies

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...

You might also read

Related Articles

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

Sort by

Same author

Mucosal-associated invariant T cells recognize a tumor-derived metabolite in the DNA synthesis pathway.

Frontiers in immunology·2026

Same author

Activation of AMPK as a therapeutic strategy for FBXL4-related mitochondrial DNA depletion syndrome.

EMBO molecular medicine·2026

Same author

Chronic viral infection aggravates white adipose tissue dysfunction and liver pathology in obesity.

Molecular metabolism·2026

Same author

Targeting hypothalamic SIK3 to promote weight loss and improve glycemic control in mice.

Nature communications·2026

Same author

Environmental sound perception in individuals with hearing loss: A systematic review.

Auris, nasus, larynx·2026

Same author

Andexanet Alfa for Life-Threatening Bleeding Following Factor Xa Inhibitor Treatment: Postmarketing Surveillance Study in Japan.

JACC. Asia·2026

Search research articles

Related Experiment Video

Updated: Jun 27, 2026

Quantification of Endosome and Lysosome Motilities in Cultured Neurons Using Fluorescent Probes

Quantification of Endosome and Lysosome Motilities in Cultured Neurons Using Fluorescent Probes

Published on: May 22, 2017

Regulating the motor for GLUT4 vesicle traffic.

Geoffrey D Holman¹, Kei Sakamoto

¹Department of Biology and Biochemistry, University of Bath, Bath, UK. g.d.holman@bath.ac.uk

Cell Metabolism

|December 3, 2008

Summary

Insulin signaling activates the GLUT4 glucose transporter by triggering vesicle movement. Yip et al. (2008) show that myosin-1c is phosphorylated by CaMKII, linking this motor protein to insulin

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Insulin signaling regulates glucose uptake through the translocation of GLUT4 vesicles to the plasma membrane.
This process involves complex mechanical events and multiprotein machinery.
The precise molecular mechanisms coordinating vesicle trafficking remain under investigation.

Discussion:

Yip et al. (2008) identify myosin-1c as a novel component in insulin signaling.
They demonstrate direct phosphorylation of myosin-1c by Ca2+/calmodulin-dependent protein kinase II (CaMKII).
This phosphorylation event links a key motor protein to the insulin-stimulated glucose transporter trafficking pathway.

Key Insights:

Myosin-1c is a direct target of CaMKII in the context of insulin signaling.

More Related Videos

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Published on: March 7, 2018

An Antibody Feeding Approach to Study Glutamate Receptor Trafficking in Dissociated Primary Hippocampal Cultures

An Antibody Feeding Approach to Study Glutamate Receptor Trafficking in Dissociated Primary Hippocampal Cultures

Published on: August 2, 2019

Related Experiment Videos

Last Updated: Jun 27, 2026

Quantification of Endosome and Lysosome Motilities in Cultured Neurons Using Fluorescent Probes

Quantification of Endosome and Lysosome Motilities in Cultured Neurons Using Fluorescent Probes

Published on: May 22, 2017

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Published on: March 7, 2018

An Antibody Feeding Approach to Study Glutamate Receptor Trafficking in Dissociated Primary Hippocampal Cultures

An Antibody Feeding Approach to Study Glutamate Receptor Trafficking in Dissociated Primary Hippocampal Cultures

Published on: August 2, 2019

Phosphorylation of myosin-1c by CaMKII plays a role in GLUT4 vesicle trafficking.

This finding provides a mechanistic link between calcium signaling and glucose transporter regulation.

Outlook:

Further research can elucidate the specific functional consequences of myosin-1c phosphorylation on vesicle dynamics.
Investigating the interplay between myosin-1c and other components of the trafficking machinery.
Exploring potential therapeutic strategies targeting this pathway for metabolic disorders.