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Clathrin Light ChainsClathrin Heavy ChainsClathrinClathrin-Coated VesiclesCoated Pits, Cell-MembraneEndocytosisCattleAdaptor Proteins, Vesicular TransportMonomeric Clathrin Assembly ProteinsBrain ChemistryMolecular Sequence DataAmino Acid SequenceAuxilinsImmunoglobulin Light ChainsAdaptor Protein Complex 2Protein BindingMyosin Light ChainsMyosin Heavy ChainsImmunoglobulin Heavy ChainsCoated VesiclesMicroscopy, FluorescenceAdaptor Protein Complex alpha SubunitsLightAdaptor Protein Complex 1DynaminsEndosomestrans-Golgi NetworkMacromolecular SubstancesAdaptor Protein Complex beta Subunits

VesiclesAdaptor proteinsInteractsTriskelionRecruitsVesiclePitsMembraneCoatStructuralPrimarilyInteractionOrganellesMainRoleAssemblyAdaptor proteinMotifsProteinDomain

Vesicles11

• Clathrin is a protein that plays a major role in the formation of coated vesicles. (wikipedia.org)
• Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. (wikipedia.org)
• Clathrin performs critical roles in shaping rounded vesicles in the cytoplasm for intracellular trafficking. (wikipedia.org)
• Clathrin-coated vesicles (CCVs) selectively sort cargo at the cell membrane, trans-Golgi network, and endosomal compartments for multiple membrane traffic pathways. (wikipedia.org)
• Epsin also recruits clathrin to membranes and promotes its polymerization, and can help deform the membrane, and thus clathrin-coated vesicles can bud. (wikipedia.org)
• In non-dividing cells, the formation of clathrin-coated vesicles occurs continuously. (wikipedia.org)
• The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. (lookformedical.com)
• Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES. (lookformedical.com)
• An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE. (lookformedical.com)
• The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS. (lookformedical.com)
• Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. (lookformedical.com)

Adaptor proteins2

• Clathrin cannot bind to membrane or cargo directly and instead uses adaptor proteins to do this. (wikipedia.org)
• Two examples of adaptor proteins are AP180 and epsin. (wikipedia.org)

Interacts1

• Clathrin also interacts with cytoskeletal proteins. (lookformedical.com)

Triskelion4

• It forms a triskelion shape composed of three clathrin heavy chains and three light chains. (wikipedia.org)
• The clathrin triskelion is composed of three clathrin heavy chains interacting at their C-termini, each ~190 kDa heavy chain has a ~25 kDa light chain tightly bound to it. (wikipedia.org)
• In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three feet to the membrane at a time. (wikipedia.org)
• Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. (lookformedical.com)

Recruits1

• It recruits clathrin to membranes and also promotes its polymerization. (wikipedia.org)

Vesicle1

• After a vesicle buds into the cytoplasm, the coat rapidly disassembles, allowing the clathrin to recycle while the vesicle gets transported to a variety of locations. (wikipedia.org)

Pits1

• Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. (lookformedical.com)

Membrane1

• They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. (lookformedical.com)

Coat1

• The smallest clathrin cage commonly imaged, called a mini-coat, has 12 pentagons and only two hexagons. (wikipedia.org)

Structural2

• The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to regulate the formation and disassembly of a clathrin lattice. (wikipedia.org)
• This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs. (wikipedia.org)

Primarily2

• The light chains bind primarily to the proximal leg portion of the heavy chain with some interaction near the trimerization domain. (wikipedia.org)
• A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK. (lookformedical.com)

Interaction1

• The β-propeller at the 'foot' of clathrin contains multiple binding sites for interaction with other proteins. (wikipedia.org)

Organelles1

• Clathrin has another function aside from the coating of organelles. (wikipedia.org)

Main1

• The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells. (wikipedia.org)

Role1

• A family of proteins that play a role as cofactors in the process of CLATHRIN recycling in cells. (lookformedical.com)

Assembly1

• A subclass of clathrin assembly proteins that occur as monomers. (lookformedical.com)

Adaptor protein1

• In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three feet to the membrane at a time. (wikipedia.org)

Motifs1

• This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs. (wikipedia.org)

Protein1

• Clathrin is a protein that plays a major role in the formation of coated vesicles. (wikipedia.org)

Domain2

• Clathrin heavy chain is often described as a leg, with subdomains, representing the foot (the N-terminal domain), followed by the ankle, distal leg, knee, proximal leg, and trimerization domains. (wikipedia.org)
• The light chains bind primarily to the proximal leg portion of the heavy chain with some interaction near the trimerization domain. (wikipedia.org)