TNF receptor type 1

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TNF receptor type 1
TNF receptor type 1
after 1EXT

Existing structure data : 1EXT , 1FT4 , 1ICH , 1NCF , 1TNR

Mass / length primary structure 55 kilodaltons
Identifier
External IDs

The tumor necrosis factor receptor type 1 (abbreviation: TNFR1 ) is a receptor of the TNF receptor superfamily and is involved in programmed cell death and inflammatory processes. The type 1 TNF receptor has a molar mass of around 55 kilodaltons and is therefore also called p55TNF-R receptor ( p55TNFR ). In the nomenclature of the differentiation markers of the cell surface ( cluster of differentiation ) it corresponds to the CD120a .

function

A long-known function of this TNF receptor is the induction of programmed cell death ( apoptosis ). However, the receptor can also develop anti-apoptotic effects. It is also important in processes of acute and chronic inflammatory reactions. The effect of the receptor depends on a number of complex regulatory mechanisms.

Gene expression

Most cell lines in the human body carry the TNF receptor of type 1. The gene of this receptor is constitutively expressed (in contrast to that of the TNF receptor type 2 ) . In humans, it is on chromosome 12 (12p13).

structure

The TNF receptor type 1 is, like all other (so far 29) members of the TNF receptor superfamily, a transmembrane protein of type 1, i.e. a protein with an intracellularly localized C terminus . As another typical characteristic of the superfamily, the receptor has several (in this case three) extracellular cysteine- rich protein domains (CRD). At the intracellular carboxy-terminal portion of the receptor carries a so-called death domain ( english death domain , DD). It therefore belongs to the subgroup of death receptors.

Signal transduction

The most important ligand for this receptor is tumor necrosis factor . The receptor can bind both the soluble and the membrane-bound form of tumor necrosis factor. Both forms of tumor necrosis factor can activate the receptor and initiate signal transduction . In addition, the soluble, homotrimeric form of lymphotoxin (LTα3) and the membrane-bound, heterotrimeric form of lymphotoxin (LTα2β1) can bind to the receptor. Independent of the binding of a ligand, the TNFR1 forms a homomeric trimer . This is based on the so-called preligand assembly domain (PLAD) located at the N terminus of the individual receptor monomers and is a prerequisite for effective ligand binding.

The death domain of TNFR1 is blocked in the resting state by the inhibitory protein SODD ( silencer of death domains ), which prevents uncontrolled induction of signal transduction. If a corresponding ligand, such as tumor necrosis factor , binds to the receptor, SODD is released from the death domain of the receptor and various intracellular signal cascades can be set in motion. First, the protein TRADD ( TNFR associated protein with a death domain ) binds with its own death domain to the death domain of the receptor. Starting from this situation, depending on many factors, different protein signal complexes can in turn form and different ways of intracellular signal transduction can be set in motion, at the end of which there is a corresponding cellular reaction.

For example, the recruitment of FADD ( Fas associated protein with a death domain ) in this signal complex with subsequent activation of a caspase cascade (aspartate-specific cysteine ​​proteases) causes DNA degradation and consequently cell death . Another way of signal transduction results in the activation of transcription factors such as AP-1 (activating protein 1) and NF-κB , which in turn are involved in acute and chronic inflammation.

interaction

TNFRSF1A interacts with various proteins, e.g. B. BAG4 , CASP10 , FADD , IKK2 , JAK1 , JAK2 , PIP4K2B , PSMD2 , RIPK1 , SUMO1 , TRADD TRAF2 , TRPC4AP , TNF , and UBE2I .

Diseases

In the TNF-receptor-associated periodic fever syndrome , the number of TNF receptors is reduced.

Web links

Individual evidence

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