clathrin

The particles are absorbed through the use of clathrin coated pits.

Clathrin has another function aside from the coating of organelles.

Clathrin binds to its receptors that are present in the membrane.

The clathrin coat is thought to assemble in response to regulatory G protein.

This domain is required for binding to clathrin, and its subsequent polymerisation.

A classical example of such interactions is the activity of the protein clathrin.

It recruits clathrin to membranes and also promotes its polymerization.

Clathrin is a protein that plays a major role in the formation of coated vesicles.

Clathrin was first isolated and named by Barbara Pearse in 1975.

The clathrin coats are lost almost immediately, and the membrane is subsequently recycled to the cell surface.

Dynamin is responsible for the separation of clathrin buds from the plasma membrane.

This is an adaptor protein which helps the formation of a clathrin coat around a vesicle.

The protein contains a clathrin box, with two identified clathrin-binding motifs, and is involved in vesicle-trafficking.

Its kinase activity is stimulated by clathrin.

Coat-proteins, like clathrin, are used to build small vesicles in order to safely transport molecules within and between cells.

The clathrin proteins will then dissociate.

The major route for endocytosis in most cells, and the best-understood, is that mediated by the molecule clathrin.

During mitosis, clathrin binds to the spindle apparatus.

During mitosis the clathrin binds directly to the microtubules or microtubule-associated proteins.

The clathrin-binding domain gathers clathrin into baskets.

Pearse first purified coated vesicles; she also discovered the clathrin coat molecule in 1975.

Clathrin is involved in cellular exocytosis and is sequestrated by specific signaling molecules.

The alpha and beta appendage domains bind to accessory proteins and to clathrin.

It has been previously suggested that gap junction plaque internalization is mediated by clathrin and its associated proteins.

It forms a triskelion shape composed of three clathrin heavy chains and three light chains.