The lack of an ordered structure can facilitate a kind of functional promiscuity, allowing one protein to interact with multiple partners. Some intrinsically disordered proteins act to inhibit the action of other proteins by an unusual mechanism: wrapping around their protein targets.

TLS Online TPP Program

#Id: 9625

#XL - T Zoology

Unbound receptors are internalized at a relatively slow rate, on average once every 30 minutes, and are recycled rapidly to the plasma membrane so there is little reduction in the total number of surface receptors. 

TLS Online TPP Program

#Id: 9626

#XL - T Zoology

Following binding of an EGF ligand, the rate of endocytosis of HER1 is increased about tenfold, and only a fraction of the internalized receptors return to the plasma membrane; the rest are degraded in lysosomes.

TLS Online TPP Program

#Id: 9627

#XL - T Zoology

Monoubiquitinylation of the HER1 cytosolic domain by the E3 ubiquitin ligase c-Cbl

TLS Online TPP Program

#Id: 9628

#XL - T Zoology

c-Cbl 

adds a single ubiquitin to a given lysine of a protein

TLS Online TPP Program

#Id: 9629

#XL - T Zoology

c-Cbl contains: 

a domain that binds directly to phosphorylated EGF receptors

a RING finger domain, which recruits ubiquitin-conjugating enzymes and mediates transfer of ubiquitin to the receptor

TLS Online TPP Program

#Id: 9630

#XL - T Zoology

Other EGF family receptors HER2, HER3, and HER4 do not undergo internalization after exposure to ligand