Clathrin Heavy Chain
Clathrin Heavy Chain - Related Videos
17:14
In vivo and in vitro Studies of Adaptor-clathrin Interaction
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Cited by 8 •
2011
Clathrin-mediated endocytosis depends on adaptor proteins that coordinate cargo selection and clathrin coat assembly. Here we describe procedures to study adaptor-clathrin physical interaction and live cell imaging approaches using as a model the yeast endocytic adaptor protein Sla1p.
01:12
Clathrin Coated Vesicles
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2023
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...
15:07
VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma
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Cited by 19 •
2015
This protocol describes an approach to interrogate the recombined immunoglobulin heavy chain VDJ regions of lymphomas by deep-sequencing and retrieve VDJ rearrangement and somatic hypermutation status to delineate clonal architecture of individual tumor. Comparing clonal architecture between paired diagnosis and relapse samples reveals lymphoma relapse clonal evolution modes.
10:20
Quantification of Heavy Metals and Other Inorganic Contaminants on the Productivity of Microalgae
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Cited by 14 •
2015
Integration of microalgal cultivation with industrial flue gas will ultimately introduce heavy metals and other inorganic compounds into the growth media. This study presents a procedure used to determine the end fate and impact of heavy metals and inorganic contaminants on the growth of Nannochloropsis salina grown in photobioreactors.
05:57
A Rapid Automated Protocol for Muscle Fiber Population Analysis in Rat Muscle Cross Sections Using Myosin Heavy Chain Immunohistochemistry
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Cited by 13 •
2017
Here, we present a protocol for rapid muscle fiber analyses, which allows improved staining quality, and thereby automatic acquisition and quantification of fiber populations using the freely available software ImageJ.
FAQs
Three clathrin heavy chains associate with three light chains to produce a triskelion, a structural unit that can organize into a lattice on the cytosolic membrane surface. This lattice provides an ordered coat as a membrane region bends and matures into a vesicle. The arrangement links protein assembly with the physical remodeling required for intracellular trafficking.
Clathrin light chains participate in forming the triskelion with the heavy chains, while adaptor proteins connect the coat to selected cargo and membrane components. These relationships help coordinate coat assembly with cargo selection rather than allowing membrane remodeling to occur independently. Consequently, the system supports organized uptake and sorting of particular receptors or other transported material.
The lattice forms on the cytosolic surface of the membrane, positioning the coat where it can interact with adaptor proteins and membrane-associated cargo. This orientation allows the coat to coordinate the inward remodeling of the membrane while adaptors link selected cargo to the assembling structure. The result is a membrane bud prepared for vesicle formation and subsequent trafficking.
At the plasma membrane, clathrin-coated pits typically support endocytosis, bringing selected material into the cell. At the trans-Golgi network, the same coat system contributes to trafficking from an internal sorting compartment. Comparing these locations helps distinguish how one structural machinery participates in receptor uptake at the cell surface and cargo movement through intracellular pathways.
A useful investigation can examine triskelion assembly, lattice organization, adaptor connections, and the formation or maturation of clathrin-coated pits. It can then relate these structural features to receptor uptake, cargo sorting, and membrane recycling. This progression connects molecular organization with cellular transport outcomes without treating coat formation as an isolated structural event.
Studying Clathrin Heavy Chain provides a framework for investigating receptor uptake, cargo sorting, membrane recycling, and vesicle transport. It is also relevant when examining how defects in intracellular trafficking disrupt cellular function. These applications connect the protein's structural role to broader questions about how cells maintain membrane composition and distribute material between cellular compartments.